EC |
2.4.1.229 | Relevance: 100% |
Accepted name: |
[Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + [Skp1-protein]-trans-4-hydroxy-L-proline = UDP + [Skp1-protein]-O-(N-acetyl-α-D-glucosaminyl)-trans-4-hydroxy-L-proline |
Other name(s): |
Skp1-HyPro GlcNAc-transferase; UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase; UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase; UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:[Skp1-protein]-trans-4-hydroxy-L-proline N-acetyl-α-D-glucosaminyl-transferase |
Comments: |
Skp1 is a cytoplasmic and nuclear protein required for the ubiquitination of cell cycle regulatory proteins and transcriptional factors. In Dictyostelium Skp1 is modified by the linear pentasaccharide Galα1-6Galα1-L-Fucα1-2Galβ1-3GlcNAc, which is attached to a hydroxyproline residue at position 143. This enzyme catalyses the first step in the building up of the pentasaccharide by attaching an N-acetylglucosaminyl group to the hydroxyproline residue. It requires dithiothreitol and a divalent cation for activity. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 256531-81-4 |
References: |
1. |
van der Wel, H., Morris, H.R., Panico, M., Paxton, T., Dell, A., Kaplan, L. and West, C.M. Molecular cloning and expression of a UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase that modifies Skp1 in the cytoplasm of Dictyostelium. J. Biol. Chem. 277 (2002) 46328–46337. [DOI] [PMID: 12244115] |
2. |
Teng-umnuay, P., van der Wel, H. and West, C.M. Identification of a UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase in the cytoplasm of Dictyostelium. J. Biol. Chem. 274 (1999) 36392–36402. [DOI] [PMID: 10593934] |
3. |
West, C.M., van der Wel, H. and Gaucher, E.A. Complex glycosylation of Skp1 in Dictyostelium: implications for the modification of other eukaryotic cytoplasmic and nuclear proteins. Glycobiology 12 (2002) 17. [DOI] [PMID: 11886837] |
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[EC 2.4.1.229 created 2003, modified 2013] |
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EC |
2.1.1.294 | Relevance: 98.9% |
Accepted name: |
3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + 3-O-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = S-adenosyl-L-homocysteine + 3-O-methylphospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol |
Other name(s): |
WbdD; S-adenosyl-L-methionine:3-O-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→3)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-α-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase |
Systematic name: |
S-adenosyl-L-methionine:3-O-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase |
Comments: |
The enzyme is involved in the biosynthesis of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. O-Polysaccharide structures vary extensively because of differences in the number and type of sugars in the repeat unit. The dual kinase/methylase WbdD also catalyses the preceding phosphorylation of α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol (cf. EC 2.7.1.181, polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Clarke, B.R., Cuthbertson, L. and Whitfield, C. Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter. J. Biol. Chem. 279 (2004) 35709–35718. [DOI] [PMID: 15184370] |
2. |
Clarke, B.R., Greenfield, L.K., Bouwman, C. and Whitfield, C. Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway. J. Biol. Chem. 284 (2009) 30662–30672. [DOI] [PMID: 19734145] |
3. |
Clarke, B.R., Richards, M.R., Greenfield, L.K., Hou, D., Lowary, T.L. and Whitfield, C. In vitro reconstruction of the chain termination reaction in biosynthesis of the Escherichia coli O9a O-polysaccharide: the chain-length regulator, WbdD, catalyzes the addition of methyl phosphate to the non-reducing terminus of the growing glycan. J. Biol. Chem. 286 (2011) 41391–41401. [DOI] [PMID: 21990359] |
4. |
Liston, S.D., Clarke, B.R., Greenfield, L.K., Richards, M.R., Lowary, T.L. and Whitfield, C. Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen. J. Biol. Chem. 290 (2015) 1075–1085. [DOI] [PMID: 25422321] |
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[EC 2.1.1.294 created 2014, modified 2018] |
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EC |
2.4.1.147 | Relevance: 96.5% |
Accepted name: |
acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + O3-[N-acetyl-α-D-galactosaminyl]-L-threonyl/L-seryl-[protein] = UDP + O3-[N-acetyl-β-D-glucosaminyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-threonyl/L-seryl-[protein] |
Other name(s): |
O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III; uridine diphosphoacetylglucosamine-mucin β(1→3)-acetylglucosaminyltransferase; mucin core 3 β3-GlcNAc-transferase; Core 3β-GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosaminyl-R) β-1,3-N-acetyl-D-glucosaminyltransferase; UDP-N-acetyl-D-glucosamine:N-acetyl-β-D-galactosaminyl-R 3-β-N-acetyl-D-glucosaminyltransferase (incorrect) |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:O3-[N-acetyl-α-D-galactosaminyl]-L-threonyl/L-seryl-[protein] 3-β-N-acetyl-D-glucosaminyltransferase |
Comments: |
The product of the enzyme is known as core 3, one of the eight core structures of mucin-type O-glycans. O-Linked glycans are polysaccharides or oligosaccharides that are linked to a protein via the oxygen atom in the side chain of an L-serine or L-threonine residue. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 87927-96-6 |
References: |
1. |
Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [DOI] [PMID: 6226356] |
2. |
Brockhausen, I., Matta, K.L., Orr, J. and Schachter, H. Mucin synthesis. UDP-GlcNAc:GalNAc-R β 3-N-acetylglucosaminyltransferase and UDP-GlcNAc:GlcNAc β 1-3GalNAc-R (GlcNAc to GalNAc) β 6-N-acetylglucosaminyltransferase from pig and rat colon mucosa. Biochemistry 24 (1985) 1866–1874. [PMID: 3160388] |
3. |
Vavasseur, F., Yang, J.M., Dole, K., Paulsen, H. and Brockhausen, I. Synthesis of O-glycan core 3: characterization of UDP-GlcNAc: GalNAc-R β 3-N-acetyl-glucosaminyltransferase activity from colonic mucosal tissues and lack of the activity in human cancer cell lines. Glycobiology 5 (1995) 351–357. [DOI] [PMID: 7655172] |
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[EC 2.4.1.147 created 1984, modified 2015] |
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EC |
2.4.1.86 | Relevance: 96.3% |
Accepted name: |
N-acetyl-β-D-glucosaminide β-(1,3)-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-R = UDP + β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R |
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For diagram of lactotetraosylceramide biosynthesis, click here |
Other name(s): |
B3GALT1 (gene name); uridine diphosphogalactose-acetyl-glucosaminylgalactosylglucosylceramide galactosyltransferase; GalT-4; UDP-galactose:N-acetyl-D-glucosaminyl-1,3-D-galactosyl-1,4-D-glucosylceramide β-D-galactosyltransferase; UDP-galactose:N-acetyl-D-glucosaminyl-(1→3)-D-galactosyl-(1→4)-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase; glucosaminylgalactosylglucosylceramide β-galactosyltransferase; UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase |
Systematic name: |
UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-R 3-β-D-galactosyltransferase |
Comments: |
The enzyme transfers galactose from UDP-α-D-galactose to the 3-position of substrates with a non-reducing terminal N-acetyl-β-D-glucosamine (β-GlcNAc) residue. It can act on both glycolipids and glycoproteins, generating a structure known as the type 1 histo-blood group antigen precursor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9073-46-5 |
References: |
1. |
Basu, M. and Basu, S. Enzymatic synthesis of a tetraglycosylceramide by a galactosyltransferase from rabbit bone marrow. J. Biol. Chem. 247 (1972) 1489–1495. [PMID: 4335001] |
2. |
Basu, M., Presper, K.A., Basu, S., Hoffman, L.M. and Brooks, S.E. Differential activities of glycolipid glycosyltransferases in Tay-Sachs disease: studies in cultured cells from cerebrum. Proc. Natl. Acad. Sci. USA 76 (1979) 4270–4274. [DOI] [PMID: 291963] |
3. |
Amado, M., Almeida, R., Carneiro, F., Levery, S.B., Holmes, E.H., Nomoto, M., Hollingsworth, M.A., Hassan, H., Schwientek, T., Nielsen, P.A., Bennett, E.P. and Clausen, H. A family of human β3-galactosyltransferases. Characterization of four members of a UDP-galactose:β-N-acetyl-glucosamine/β-nacetyl-galactosamine β-1,3-galactosyltransferase family. J. Biol. Chem. 273 (1998) 12770–12778. [DOI] [PMID: 9582303] |
4. |
Amado, M., Almeida, R., Schwientek, T. and Clausen, H. Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim. Biophys. Acta 1473 (1999) 35–53. [DOI] [PMID: 10580128] |
5. |
Bardoni, A., Valli, M. and Trinchera, M. Differential expression of β1,3galactosyltransferases in human colon cells derived from adenocarcinomas or normal mucosa. FEBS Lett. 451 (1999) 75–80. [DOI] [PMID: 10356986] |
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[EC 2.4.1.86 created 1976, modified 2017] |
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EC |
2.7.8.35 | Relevance: 94.6% |
Accepted name: |
UDP-N-acetylglucosamine—decaprenyl-phosphate N-acetylglucosaminephosphotransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + trans,octacis-decaprenyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol |
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For diagram of galactofuranan biosynthesis, click here |
Other name(s): |
GlcNAc-1-phosphate transferase; UDP-GlcNAc:undecaprenyl phosphate GlcNAc-1-phosphate transferase; WecA; WecA transferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:trans,octacis-decaprenyl-phosphate N-acetylglucosaminephosphotransferase |
Comments: |
Isolated from Mycobacterium tuberculosis and Mycobacterium smegmatis. This enzyme catalyses the synthesis of monotrans,octacis-decaprenyl-N-acetyl-α-D-glucosaminyl diphosphate (mycobacterial lipid I), an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. cf. EC 2.7.8.33, UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Jin, Y., Xin, Y., Zhang, W. and Ma, Y. Mycobacterium tuberculosis Rv1302 and Mycobacterium smegmatis MSMEG_4947 have WecA function and MSMEG_4947 is required for the growth of M. smegmatis. FEMS Microbiol. Lett. 310 (2010) 54–61. [DOI] [PMID: 20637039] |
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[EC 2.7.8.35 created 2012] |
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EC |
3.2.1.96 | Relevance: 93% |
Accepted name: |
mannosyl-glycoprotein endo-β-N-acetylglucosaminidase |
Reaction: |
Endohydrolysis of the N,N′-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact |
Other name(s): |
N,N′-diacetylchitobiosyl β-N-acetylglucosaminidase; endo-β-N-acetylglucosaminidase; mannosyl-glycoprotein endo-β-N-acetylglucosamidase; di-N-acetylchitobiosyl β-N-acetylglucosaminidase; endo-β-acetylglucosaminidase; endo-β-(1→4)-N-acetylglucosaminidase; mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-D-glycohydrolase; endoglycosidase S; endo-N-acetyl-β-D-glucosaminidase; endo-N-acetyl-β-glucosaminidase; endo-β-N-acetylglucosaminidase D; endo-β-N-acetylglucosaminidase F; endo-β-N-acetylglucosaminidase H; endo-β-N-acetylglucosaminidase L; glycopeptide-D-mannosyl-4-N-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase; endoglycosidase H |
Systematic name: |
glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase |
Comments: |
A group of related enzymes. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-88-9 |
References: |
1. |
Chien, S., Weinburg, R., Li, S. and Li, Y. Endo-β-N-acetylglucosaminidase from fig latex. Biochem. Biophys. Res. Commun. 76 (1977) 317–323. [DOI] [PMID: 1027432] |
2. |
Koide, N. and Muramatsu, T. Endo-β-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae. J. Biol. Chem. 249 (1974) 4897–4904. [PMID: 4152561] |
3. |
Pierce, R.J., Spik, G. and Montreuil, J. Cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity in rat liver and kidney. Biochem. J. 180 (1979) 673. [PMID: 486141] |
4. |
Pierce, R.J., Spik, G. and Montreuil, J. Demonstration and cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver. Biochem. J. 185 (1980) 261–264. [PMID: 7378051] |
5. |
Tai, T., Yamashita, K., Ogata-Arakawa, M., Koide, N., Muramatsu, T., Iwashita, S., Inoue, Y. and Kobata, A. Structural studies of two ovalbumin glycopeptides in relation to the endo-β-N-acetylglucosaminidase specificity. J. Biol. Chem. 250 (1975) 8569–8575. [PMID: 389] |
6. |
Tarentino, A.L., Plummer, T.H., Jr. and Maley, F. The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosaminidase H. J. Biol. Chem. 249 (1974) 818–824. [PMID: 4204553] |
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[EC 3.2.1.96 created 1978] |
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EC |
5.1.3.36 | Relevance: 92.6% |
Accepted name: |
heparosan-glucuronate 5-epimerase |
Reaction: |
[heparosan]-D-glucuronate = [acharan]-L-iduronate |
Glossary: |
acharan = [GlcNAc-α-(1→4)-IdoA-α-(1→4)]n
heparosan = [GlcNAc-α-(1→4)-GlcA-β-(1→4)]n |
Other name(s): |
HG-5epi |
Systematic name: |
[heparosan]-D-glucuronate 5-epimerase |
Comments: |
The enzyme, characterized from the giant African snail Achatina fulica, participates in the biosynthetic pathway of acharan sulfate. Unlike EC 5.1.3.17, heparosan-N-sulfate-glucuronate 5-epimerase, it shows no activity with D-glucuronate residues in heparosan-N-sulfate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Mochizuki, H., Yamagishi, K., Suzuki, K., Kim, Y.S. and Kimata, K. Heparosan-glucuronate 5-epimerase: Molecular cloning and characterization of a novel enzyme. Glycobiology 25 (2015) 735–744. [DOI] [PMID: 25677302] |
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[EC 5.1.3.36 created 2015] |
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EC |
2.4.1.65 | Relevance: 92.6% |
Accepted name: |
3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase |
Reaction: |
GDP-β-L-fucose + β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R = GDP + β-D-galactosyl-(1→3)-[α-L-fucosyl-(1→4)]-N-acetyl-β-D-glucosaminyl-R |
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For diagram of reaction, click here |
Other name(s): |
(Lea)-dependent (α-3/4)-fucosyltransferase; α(1,3/1,4) fucosyltransferase III; α-(1→4)-L-fucosyltransferase; α-4-L-fucosyltransferase; β-acetylglucosaminylsaccharide fucosyltransferase; FucT-II; Lewis α-(1→3/4)-fucosyltransferase; Lewis blood group α-(1→3/4)-fucosyltransferase; Lewis(Le) blood group gene-dependent α-(1→3/4)-L-fucosyltransferase; blood group Lewis α-4-fucosyltransferase; blood-group substance Lea-dependent fucosyltransferase; guanosine diphosphofucose-β-acetylglucosaminylsaccharide 4-α-L-fucosyltransferase; guanosine diphosphofucose-glycoprotein 4-α-L-fucosyltransferase; guanosine diphosphofucose-glycoprotein 4-α-fucosyltransferase; 3-α-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase; GDP-β-L-fucose:3-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 4I-α-L-fucosyltransferase; GDP-L-fucose:3-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 4I-α-L-fucosyltransferase |
Systematic name: |
GDP-β-L-fucose:β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R 4I-α-L-fucosyltransferase (configuration-inverting) |
Comments: |
This enzyme is the product of the Lewis blood group gene. Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. Although it is a 4-fucosyltransferase, it has a persistent 3-fucosyltransferase activity towards the glucose residue in free lactose. This enzyme fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3, unlike EC 2.4.1.152, 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase, which fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4. Enzymes catalysing the 4-α-fucosylation of the GlcNAc in β-D-Gal-(1→3)-β-GlcNAc sequences (with some activity also as 3-α-fucosyltransferases) are present in plants, where the function in vivo is the modification of N-glycans. In addition, the fucTa gene of Helicobacter strain UA948 encodes a fucosyltransferase with both 3-α- and 4-α-fucosyltransferase activities. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-69-3 |
References: |
1. |
Prieels, J.-P., Monnom, D., Dolmans, M., Beyer, T.A. and Hill, R.L. Co-purification of the Lewis blood group N-acetylglucosaminide α1→4 fucosyltransferase and an N-acetylglucosaminide α1→3 fucosyltransferase from human milk. J. Biol. Chem. 256 (1981) 10456–10463. [PMID: 7287719] |
2. |
Rasko, D.A., Wang, G., Palcic, M.M. and Taylor, D.E. Cloning and characterization of the α(1,3/4) fucosyltransferase of Helicobacter pylori. J. Biol. Chem. 275 (2000) 4988–4994. [DOI] [PMID: 10671538] |
3. |
Wilson, I.B.H. Identification of a cDNA encoding a plant Lewis-type α1,4-fucosyltransferase. Glycoconj. J. 18 (2001) 439–447. [PMID: 12084979] |
4. |
Ma, B., Wang, G., Palcic, M.M., Hazes, B. and Taylor, D.E. C-terminal amino acids of Helicobacter pylori α1,3/4
fucosyltransferases determine type I and type II transfer. J. Biol. Chem. 278 (2003) 21893–21900. [DOI] [PMID: 12676935] |
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[EC 2.4.1.65 created 1972, modified 2001, modified twice 2002] |
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EC |
3.2.1.97 | Relevance: 92.1% |
Accepted name: |
endo-α-N-acetylgalactosaminidase |
Reaction: |
β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-[glycoprotein]-L-serine/L-threonine + H2O = β-D-galactosyl-(1→3)-N-acetyl-D-galactosamine + [glycoprotein]-L-serine/L-threonine |
Other name(s): |
endo-α-acetylgalactosaminidase; endo-α-N-acetyl-D-galactosaminidase; mucinaminylserine mucinaminidase; D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase; endo-α-GalNAc-ase; glycopeptide α-N-acetylgalactosaminidase; D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase |
Systematic name: |
glycopeptide-D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase |
Comments: |
The enzyme catalyses the liberation of Gal-(1→3)-β-GalNAc α-linked to serine or threonine residues of mucin-type glycoproteins. EngBF from the bacterium Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1→3)-β-GalNAc. The enzymes from the bacteria Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. they can also release the core 2 trisaccharide Gal-(1→3)-β-(GlcNAc-(1→6)-β)-GalNAc or the core 3 disaccharide GlcNAc-(1→3)-β-GalNAc) [1,2]. The enzyme may play an important role in the degradation and utilization of mucins having core 1 O-glycan. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 59793-96-3 |
References: |
1. |
Ashida, H., Maki, R., Ozawa, H., Tani, Y., Kiyohara, M., Fujita, M., Imamura, A., Ishida, H., Kiso, M. and Yamamoto, K. Characterization of two different endo-α-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens. Glycobiology 18 (2008) 727–734. [DOI] [PMID: 18559962] |
2. |
Koutsioulis, D., Landry, D. and Guthrie, E.P. Novel endo-α-N-acetylgalactosaminidases with broader substrate specificity. Glycobiology 18 (2008) 799–805. [DOI] [PMID: 18635885] |
3. |
Fujita, K., Oura, F., Nagamine, N., Katayama, T., Hiratake, J., Sakata, K., Kumagai, H. and Yamamoto, K. Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-α-N-acetylgalactosaminidase from Bifidobacterium longum. J. Biol. Chem. 280 (2005) 37415–37422. [DOI] [PMID: 16141207] |
4. |
Suzuki, R., Katayama, T., Kitaoka, M., Kumagai, H., Wakagi, T., Shoun, H., Ashida, H., Yamamoto, K. and Fushinobu, S. Crystallographic and mutational analyses of substrate recognition of endo-α-N-acetylgalactosaminidase from Bifidobacterium longum. J. Biochem. 146 (2009) 389–398. [DOI] [PMID: 19502354] |
5. |
Gregg, K.J. and Boraston, A.B. Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of a family 101 glycoside hydrolase from Streptococcus pneumoniae. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 (2009) 133–135. [DOI] [PMID: 19194003] |
6. |
Ashida, H., Yamamoto, K., Murata, T., Usui, T. and Kumagai, H. Characterization of endo-α-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity. Arch. Biochem. Biophys. 373 (2000) 394–400. [DOI] [PMID: 10620364] |
7. |
Goda, H.M., Ushigusa, K., Ito, H., Okino, N., Narimatsu, H. and Ito, M. Molecular cloning, expression, and characterization of a novel endo-α-N-acetylgalactosaminidase from Enterococcus faecalis. Biochem. Biophys. Res. Commun. 375 (2008) 441–446. [DOI] [PMID: 18725192] |
|
[EC 3.2.1.97 created 1978 (EC 3.2.1.110 created 1984, incorporated 2008), modified 2008, modified 2011] |
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|
EC |
2.4.1.244 | Relevance: 89.3% |
Accepted name: |
N-acetyl-β-glucosaminyl-glycoprotein 4-β-N-acetylgalactosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-galactosamine + N-acetyl-β-D-glucosaminyl group = UDP + N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group |
Glossary: |
N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosamine = N,N′-diacetyllactosediamine |
Other name(s): |
β1,4-N-acetylgalactosaminyltransferase III; β4GalNAc-T3; β1,4-N-acetylgalactosaminyltransferase IV; β4GalNAc-T4; UDP-N-acetyl-D-galactosamine:N-acetyl-D-glucosaminyl-group β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetyl-β-D-glucosaminyl-group 4-β-N-acetylgalactosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-group 4-β-N-acetylgalactosaminyltransferase |
Comments: |
The enzyme from human can transfer N-acetyl-D-galactosamine (GalNAc) to N-glycan and O-glycan substrates that have N-acetyl-D-glucosamine (GlcNAc) but not D-glucuronic acid (GlcUA) at their non-reducing end. The N-acetyl-β-D-glucosaminyl group is normally on a core oligosaccharide although benzyl glycosides have been used in enzyme-characterization experiments. Some glycohormones, e.g. lutropin and thyrotropin contain the N-glycan structure containing the N-acetyl-β-D-galactosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl group. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Sato, T., Gotoh, M., Kiyohara, K., Kameyama, A., Kubota, T., Kikuchi, N., Ishizuka, Y., Iwasaki, H., Togayachi, A., Kudo, T., Ohkura, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of a novel human β1,4-N-acetylgalactosaminyltransferase, β4GalNAc-T3, responsible for
the synthesis of N,N'-diacetyllactosediamine, GalNAc β1-4GlcNAc. J. Biol. Chem. 278 (2003) 47534–47544. [DOI] [PMID: 12966086] |
2. |
Gotoh, M., Sato, T., Kiyohara, K., Kameyama, A., Kikuchi, N., Kwon, Y.D., Ishizuka, Y., Iwai, T., Nakanishi, H. and Narimatsu, H. Molecular cloning and characterization of
β1,4-N-acetylgalactosaminyltransferases IV synthesizing
N,N'-diacetyllactosediamine. FEBS Lett. 562 (2004) 134–140. [DOI] [PMID: 15044014] |
|
[EC 2.4.1.244 created 2006] |
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EC |
4.2.2.1 | Relevance: 89.1% |
Accepted name: |
hyaluronate lyase |
Reaction: |
Cleaves hyaluronate chains at a β-D-GlcNAc-(1→4)-β-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-β-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine. |
Other name(s): |
hyaluronidase (ambiguous); glucuronoglycosaminoglycan lyase (ambiguous); spreading factor; mucinase (ambiguous) |
Systematic name: |
hyaluronate lyase |
Comments: |
The enzyme catalyses the degradation of hyaluronan by a β-elimination reaction. Also acts on chondroitin. The product is more systematically known as 3-(4-deoxy-α-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37259-53-3 |
References: |
1. |
Linker, A., Hoffman, P., Meyer, K., Sampson, P. and Korn, E.D. The formation of unsaturated disacharides from mucopoly-saccharides and their cleavage to α-keto acid by bacterial enzymes. J. Biol. Chem. 235 (1960) 3061. [PMID: 13762462] |
2. |
Meyer, K. and Rapport, M.M. Hyaluronidases. Adv. Enzymol. Relat. Subj. Biochem. 13 (1952) 199–236. [PMID: 14943668] |
3. |
Moran, F., Nasuno, S. and Starr, M.P. Extracellular and intracellular polygalacturonic acid trans-eliminases of Erwinia carotovora. Arch. Biochem. Biophys. 123 (1968) 298–306. [DOI] [PMID: 5642600] |
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[EC 4.2.2.1 created 1961 as EC 4.2.99.1, transferred 1972 to EC 4.2.2.1, modified 2001] |
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EC |
3.5.1.52 | Relevance: 86.5% |
Accepted name: |
peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase |
Reaction: |
Hydrolysis of an N4-(acetyl-β-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-β-D-glucosaminylamine and a peptide containing an aspartate residue |
Other name(s): |
glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; Jack-bean glycopeptidase; PNGase A; PNGase F |
Systematic name: |
N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase |
Comments: |
Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26, N4-(β-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83534-39-8 |
References: |
1. |
Plummer, T.H., Jr. and Tarentino, A.L. Facile cleavage of complex oligosaccharides from glycopeptides by almond emulsin peptide: N-glycosidase. J. Biol. Chem. 256 (1981) 10243–10246. [PMID: 7287707] |
2. |
Takahashi, N. Demonstration of a new amidase acting on glycopeptides. Biochem. Biophys. Res. Commun. 76 (1977) 1194–1201. [DOI] [PMID: 901470] |
3. |
Takahashi, N. and Nishibe, H. Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages. J. Biochem. (Tokyo) 84 (1978) 1467–1473. [PMID: 738997] |
4. |
Tarentino, A.L., Gomez, C.M. and Plummer, T.H., Jr. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry 24 (1985) 4665–4671. [PMID: 4063349] |
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[EC 3.5.1.52 created 1984, modified 1989 (EC 3.2.2.18 created 1984, incorporated 1989)] |
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EC |
2.4.1.87 | Relevance: 84.8% |
Accepted name: |
N-acetyllactosaminide 3-α-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + β-D-galactosyl-(1→4)-β-N-acetyl-D-glucosaminyl-R = UDP + α-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-N-acetylglucosaminyl-R (where R can be OH, an oligosaccharide or a glycoconjugate) |
Other name(s): |
α-galactosyltransferase; UDP-Gal:β-D-Gal(1,4)-D-GlcNAc α(1,3)-galactosyltransferase; UDP-Gal:N-acetyllactosaminide α(1,3)-galactosyltransferase; UDP-Gal:N-acetyllactosaminide α-1,3-D-galactosyltransferase; UDP-Gal:Galβ1→4GlcNAc-R α1→3-galactosyltransferase; UDP-galactose-acetyllactosamine α-D-galactosyltransferase; UDPgalactose:β-D-galactosyl-β-1,4-N-acetyl-D-glucosaminyl-glycopeptide α-1,3-D-galactosyltransferase; glucosaminylglycopeptide α-1,3-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine α1→3-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine galactosyltransferase; uridine diphosphogalactose-galactosylacetylglucosaminylgalactosylglucosylceramide galactosyltransferase; β-D-galactosyl-N-acetylglucosaminylglycopeptide α-1,3-galactosyltransferase; UDP-galactose:N-acetyllactosaminide 3-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-1,4-β-N-acetyl-D-glucosaminyl-R 3-α-D-galactosyltransferase; UDP-galactose:β-D-galactosyl-(1→4)-β-N-acetyl-D-glucosaminyl-R 3-α-D-galactosyltransferase |
Systematic name: |
UDP-α-D-galactose:β-D-galactosyl-(1→4)-β-N-acetyl-D-glucosaminyl-R 3-α-D-galactosyltransferase |
Comments: |
Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-α1-acid glycoprotein and N-acetyllactosamine (β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine), but not on 2′-fucosylated-N-acetyllactosamine. The non-reducing terminal N-acetyllactosamine residues of glycoproteins can also act as acceptor. Now includes EC 2.4.1.124 and EC 2.4.1.151. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 128449-51-4 |
References: |
1. |
Basu, M. and Basu, S. Enzymatic synthesis of a blood group B-related pentaglycosylceramide by an α-galactosyltransferase from rabbit bone marrow. J. Biol. Chem. 248 (1973) 1700–1706. [PMID: 4632915] |
2. |
Blanken, W.M. and van den Eijnden, D.H. Biosynthesis of terminal Gal α 1→3Gal β 1→4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide α 1→3-galactosyltransferase from calf thymus. J. Biol. Chem. 260 (1985) 12927–12934. [PMID: 3932335] |
3. |
Blake, D.A. and Goldstein, I.J. An α-D-galactosyltransferase activity in Ehrlich ascites tumor cells. Biosynthesis and characterization of a trisaccharide (α-D-galactose-(1→3)-N-acetyllactosamine). J. Biol. Chem. 256 (1981) 5387–5393. [PMID: 6787040] |
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[EC 2.4.1.87 created 1976, modified 1989, modified 2002 (EC 2.4.1.124 created 1984, incorporated 2002, EC 2.4.1.151 created 1984, incorporated 2002)] |
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|
EC |
2.7.8.33 | Relevance: 84% |
Accepted name: |
UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol |
Glossary: |
N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = lipid I = GlcNAc-pyrophosphorylundecaprenol = ditrans,octacis-undecaprenyl-N-acetyl-α-D-glucosaminyl diphosphate |
Other name(s): |
UDP-N-acetylglucosamine:undecaprenyl-phosphate GlcNAc-1-phosphate transferase; WecA; WecA transferase; UDP-GIcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase; GlcNAc-P-P-Und synthase; GPT (ambiguous); TagO; UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase; UDP-N-acetyl-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetylglucosaminephosphotransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-α-D-glucosaminephosphotransferase |
Comments: |
This enzyme catalyses the synthesis of N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol, an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. The enzyme also initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide in certain Escherichia coli strains, including K-12 [2] and of teichoic acid in certain Gram-positive bacteria [4]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Al-Dabbagh, B., Mengin-Lecreulx, D. and Bouhss, A. Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA. J. Bacteriol. 190 (2008) 7141–7146. [DOI] [PMID: 18723618] |
2. |
Lehrer, J., Vigeant, K.A., Tatar, L.D. and Valvano, M.A. Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide. J. Bacteriol. 189 (2007) 2618–2628. [DOI] [PMID: 17237164] |
3. |
Rush, J.S., Rick, P.D. and Waechter, C.J. Polyisoprenyl phosphate specificity of UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase from E.coli. Glycobiology 7 (1997) 315–322. [DOI] [PMID: 9134438] |
4. |
Soldo, B., Lazarevic, V. and Karamata, D. tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168. Microbiology 148 (2002) 2079–2087. [DOI] [PMID: 12101296] |
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[EC 2.7.8.33 created 2011] |
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EC |
2.4.1.79 | Relevance: 79.5% |
Accepted name: |
globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-galactosamine + α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
|
For diagram of globotetraosylceramide biosynthesis, click here. For diagram of reaction, click here |
Glossary: |
α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = globotriaosylceramide = Pk antigen
N-acetyl-β-D-galactosaminyl-(1→3)-α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = globotetraosylceramide = globoside = P antigen |
Other name(s): |
uridine diphosphoacetylgalactosamine-galactosylgalactosylglucosylceramide acetylgalactosaminyltransferase; globoside synthetase; UDP-N-acetylgalactosamine:globotriaosylceramide β-3-N-acetylgalactosaminyltransferase; galactosylgalactosylglucosylceramide β-D-acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine:globotriaosylceramide β1,3-N-acetylgalactosaminyltransferase; globoside synthase; gUDP-N-acetyl-D-galactosamine:D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide β-N-acetyl-D-galactosaminyltransferase; β3GalNAc-T1; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosylceramide 3III-β-N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3III-β-N-acetyl-D-galactosaminyltransferase; UDP-N-acetyl-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide III3-β-N-acetyl-D-galactosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-galactosamine:α-D-galactosyl-(1→4)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide III3-β-N-acetyl-D-galactosaminyltransferase |
Comments: |
Globoside is a neutral glycosphingolipid in human erythrocytes and has blood-group-P-antigen activity [4]. The enzyme requires a divalent cation for activity, with Mn2+ required for maximal activity [3]. UDP-GalNAc is the only sugar donor that is used efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low enzyme activity [3]. Lactosylceramide, globoside and gangliosides GM3 and GD3 are not substrates [4]. For explanation of the superscripted ’3′ in the systematic name, see GL-5.3.4. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-46-1 |
References: |
1. |
Chien, J.-L., Williams, T. and Basu, S. Biosynthesis of a globoside-type glycosphingolipid by a β-N-acetylgalactosaminyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1778–1785. [PMID: 4632917] |
2. |
Ishibashi, T., Kijimoto, S. and Makita, A. Biosynthesis of globoside and Forssman hapten from trihexosylceramide and properties of β-N-acetyl-galactosaminyltransferase of guinea pig kidney. Biochim. Biophys. Acta 337 (1974) 92–106. [DOI] [PMID: 4433547] |
3. |
Taniguchi, N. and Makita, A. Purification and characterization of UDP-N-acetylgalactosamine:
globotriaosylceramide β-3-N-acetylgalactosaminyltransferase, a synthase
of human blood group P antigen, from canine spleen. J. Biol. Chem. 259 (1984) 5637–5642. [PMID: 6425294] |
4. |
Okajima, T., Nakamura, Y., Uchikawa, M., Haslam, D.B., Numata, S.I., Furukawa, K., Urano, T. and Furukawa, K. Expression cloning of human globoside synthase cDNAs. Identification of β3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide β1,3-N-acetylgalactosaminyltransferase. J. Biol. Chem. 275 (2000) 40498–40503. [DOI] [PMID: 10993897] |
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[EC 2.4.1.79 created 1976, modified 2006] |
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EC |
2.3.2.18 | Relevance: 78.6% |
Accepted name: |
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase |
Reaction: |
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 glycyl-tRNAGly = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-penta-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 tRNAGly |
Other name(s): |
femB (gene name); N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase |
Systematic name: |
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc:glycine glycyltransferase |
Comments: |
This Staphylococcus aureus enzyme catalyses the successive transfer of two Gly moieties from charged tRNAs to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphosphoundecaprenyl-GlcNAc, attaching them to the three Gly molecules that were previously attached to the N6 of the L-Lys at position 3 of the pentapeptide by EC 2.3.2.16 (lipid II:glycine glycyltransferase) and EC 2.3.2.17 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase). This is the last step in the synthesis of the pentaglycine interpeptide bridge that is used in this organism for the crosslinking of different glycan strands to each other. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ehlert, K., Schroder, W. and Labischinski, H. Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation. J. Bacteriol. 179 (1997) 7573–7576. [DOI] [PMID: 9393725] |
2. |
Rohrer, S. and Berger-Bachi, B. Application of a bacterial two-hybrid system for the analysis of protein-protein interactions between FemABX family proteins. Microbiology 149 (2003) 2733–2738. [DOI] [PMID: 14523106] |
3. |
Schneider, T., Senn, M.M., Berger-Bachi, B., Tossi, A., Sahl, H.G. and Wiedemann, I. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 53 (2004) 675–685. [DOI] [PMID: 15228543] |
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[EC 2.3.2.18 created 2010] |
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|
EC |
2.4.1.102 | Relevance: 78.6% |
Accepted name: |
β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + O3-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-seryl/threonyl-[protein] = UDP + O3-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein] |
Glossary: |
core 1 = O3-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-L-seryl/threonyl-[protein]
core 2 = O3-{β-D-galactosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→6)]-N-acetyl-α-D-galactosaminyl}-L-seryl/threonyl-[protein] |
Other name(s): |
O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; β6-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-mucin β-(1→6)-acetylglucosaminyltransferase; core 2 acetylglucosaminyltransferase; core 6-β-GlcNAc-transferase A; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of β-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R) β-1,6-N-acetyl-D-glucosaminyltransferase; GCNT1; GCNT3; UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein (N-acetyl-D-glucosamine to N-acetyl-D-galactosamine of β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl-R) 6-β-N-acetyl-D-glucosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:O3-[β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl]-glycoprotein 6-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting) |
Comments: |
The enzyme catalyses the addition of N-acetyl-α-D-glucosamine to the core 1 structure of O-glycans forming core 2. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 95978-15-7 |
References: |
1. |
Brockhausen, I., Rachaman, E.S., Matta, K.L. and Schachter, H. The separation by liquid chromatography (under elevated pressure) of phenyl, benzyl, and O-nitrophenyl glycosides of oligosaccharides. Analysis of substrates and products for four N-acetyl-D-glucosaminyl-transferases involved in mucin synthesis. Carbohydr. Res. 120 (1983) 3–16. [DOI] [PMID: 6226356] |
2. |
Williams, D., Longmore, G., Matta, K.L. and Schachter, H. Mucin synthesis. II. Substrate specificity and product identification studies on canine submaxillary gland UDP-GlcNAc:Gal β1-3GalNAc(GlcNAc→GalNAc) β6-N-acetylglucosaminyltransferase. J. Biol. Chem. 255 (1980) 11253–11261. [PMID: 6449508] |
3. |
Williams, D. and Schachter, H. Mucin synthesis. I. Detection in canine submaxillary glands of an N-acetylglucosaminyltransferase which acts on mucin substrates. J. Biol. Chem. 255 (1980) 11247–11252. [PMID: 6449507] |
|
[EC 2.4.1.102 created 1983, modified 2018] |
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|
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|
EC |
3.2.1.179 | Relevance: 78.1% |
Accepted name: |
gellan tetrasaccharide unsaturated glucuronosyl hydrolase |
Reaction: |
β-D-4-deoxy-Δ4-GlcAp-(1→4)-β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp + H2O =
5-dehydro-4-deoxy-D-glucuronate + β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp |
Glossary: |
5-dehydro-4-deoxy-D-glucuronate = (4S,5R)-4,5-dihydroxy-2,6-dioxohexanoate
β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GalNAc = 3-(4-deoxy-β-D-gluc-4-enuronosyl)-N-acetyl-D-galactosamine = 3-(4-deoxy-α-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-galactose |
Other name(s): |
UGL (ambiguous); unsaturated glucuronyl hydrolase (ambiguous); gellan tetrasaccharide unsaturated glucuronyl hydrolase |
Systematic name: |
β-D-4-deoxy-Δ4-GlcAp-(1→4)-β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp β-D-4-deoxy-Δ4-GlcAp hydrolase |
Comments: |
The enzyme releases 4-deoxy-4(5)-unsaturated D-glucuronic acid from oligosaccharides produced by polysaccharide lyases, e.g. the tetrasaccharide β-D-4-deoxy-Δ4-GlcAp-(1→4)-β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp produced by EC 4.2.2.25, gellan lyase. The enzyme can also hydrolyse unsaturated chondroitin and hyaluronate disaccharides (β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GalNAc, β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GalNAc6S, β-D-4-deoxy-Δ4-GlcAp2S-(1→3)-D-GalNAc, β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GlcNAc), preferring the unsulfated disaccharides to the sulfated disaccharides. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Itoh, T., Akao, S., Hashimoto, W., Mikami, B. and Murata, K. Crystal structure of unsaturated glucuronyl hydrolase, responsible for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 Å resolution. J. Biol. Chem. 279 (2004) 31804–31812. [DOI] [PMID: 15148314] |
2. |
Hashimoto, W., Kobayashi, E., Nankai, H., Sato, N., Miya, T., Kawai, S. and Murata, K. Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: novel enzyme prerequisite for metabolism of unsaturated oligosaccharides produced by polysaccharide lyases. Arch. Biochem. Biophys. 368 (1999) 367–374. [DOI] [PMID: 10441389] |
3. |
Itoh, T., Hashimoto, W., Mikami, B. and Murata, K. Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1. Biochem. Biophys. Res. Commun. 344 (2006) 253–262. [DOI] [PMID: 16630576] |
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[EC 3.2.1.179 created 2011, modified 2016] |
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|
EC |
2.4.1.197 | Relevance: 78.1% |
Accepted name: |
high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase |
Reaction: |
Transfers an N-acetyl-D-glucosamine residue from UDP-N-acetyl-D-glucosamine to the 4-position of a mannose linked α-(1→6) to the core mannose of high-mannose oligosaccharides produced by Dictyostelium discoideum |
Other name(s): |
uridine diphosphoacetylglucosamine-oligosaccharide acetylglucosaminyltransferase; acetylglucosamine-oligosaccharide acetylglucosaminyltransferase; UDP-GlcNAc:oligosaccharide β-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase |
Systematic name: |
UDP-N-acetyl-D-glucosamine:high-mannose-oligosaccharide 4-β-N-acetylglucosaminyltransferase |
Comments: |
The activity of the intersecting mannose residue as acceptor is dependent on two other mannose residues attached by α-1,3 and α-1,6 links. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123425-54-7 |
References: |
1. |
Sharkey, D.J. and Kornfeld, R. Identification of an N-acetylglucosaminyltransferase in Dictyostelium discoideum that transfers an "intersecting" N-acetylglucosamine residue to high mannose oligosaccharides. J. Biol. Chem. 264 (1989) 10411–10419. [PMID: 2525124] |
|
[EC 2.4.1.197 created 1992] |
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EC |
2.4.1.227 | Relevance: 76.6% |
Accepted name: |
undecaprenyldiphospho-muramoylpentapeptide β-N-acetylglucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol |
|
For diagram of peptidoglycan biosynthesis (part 2), click here |
Other name(s): |
MurG transferase; UDP-N-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol β-1,4-N-acetylglucosaminlytransferase; UDP-N-acetyl-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-β-N-acetylglucosaminlytransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:N-acetyl-α-D-muramyl(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-β-N-acetylglucosaminlytransferase (configuration-inverting) |
Comments: |
The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60976-26-3 |
References: |
1. |
van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883] |
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[EC 2.4.1.227 created 2002] |
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|
EC |
2.3.2.17 | Relevance: 76.5% |
Accepted name: |
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase |
Reaction: |
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 glycyl-tRNAGly = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 tRNAGly |
Other name(s): |
femA (gene name); N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase |
Systematic name: |
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc:glycine glycyltransferase |
Comments: |
This enzyme catalyses the successive transfer of two Gly moieties from charged tRNAs to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc, attaching them to a Gly residue previously attached by EC 2.3.2.16 (lipid II:glycine glycyltransferase) to the N6 of the L-Lys at position 3 of the pentapeptide. This is the second step in the synthesis of the pentaglycine interpeptide bridge that is used by Staphylococcus aureus for the crosslinking of different glycan strands to each other. The next step is catalysed by EC 2.3.2.18 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase). This enzyme is essential for methicillin resistance [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Berger-Bachi, B., Barberis-Maino, L., Strassle, A. and Kayser, F.H. FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus: molecular cloning and characterization. Mol. Gen. Genet. 219 (1989) 263–269. [PMID: 2559314] |
2. |
Johnson, S., Kruger, D. and Labischinski, H. FemA of Staphylococcus aureus: isolation and immunodetection. FEMS Microbiol. Lett. 132 (1995) 221–228. [DOI] [PMID: 7590176] |
3. |
Benson, T.E., Prince, D.B., Mutchler, V.T., Curry, K.A., Ho, A.M., Sarver, R.W., Hagadorn, J.C., Choi, G.H. and Garlick, R.L. X-ray crystal structure of Staphylococcus aureus FemA. Structure 10 (2002) 1107–1115. [DOI] [PMID: 12176388] |
4. |
Schneider, T., Senn, M.M., Berger-Bachi, B., Tossi, A., Sahl, H.G. and Wiedemann, I. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 53 (2004) 675–685. [DOI] [PMID: 15228543] |
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[EC 2.3.2.17 created 2010] |
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EC |
2.3.2.16 | Relevance: 76.2% |
Accepted name: |
lipid II:glycine glycyltransferase |
Reaction: |
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + glycyl-tRNAGly = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + tRNAGly |
Other name(s): |
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:N6-glycine transferase; femX (gene name); alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine:glycine N6-glycyltransferase |
Systematic name: |
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc:glycine N6-glycyltransferase |
Comments: |
The enzyme from Staphylococcus aureus catalyses the transfer of glycine from a charged tRNA to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphosphoundecaprenyl-GlcNAc (lipid II), attaching it to the N6 of the L-Lys at position 3 of the pentapeptide. This is the first step in the synthesis of the pentaglycine interpeptide bridge that is used in S. aureus for the crosslinking of different glycan strands to each other. Four additional Gly residues are subsequently attached by EC 2.3.2.17 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase) and EC 2.3.2.18 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Schneider, T., Senn, M.M., Berger-Bachi, B., Tossi, A., Sahl, H.G. and Wiedemann, I. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 53 (2004) 675–685. [DOI] [PMID: 15228543] |
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[EC 2.3.2.16 created 2010] |
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EC |
3.5.1.105 | Relevance: 73.8% |
Accepted name: |
chitin disaccharide deacetylase |
Reaction: |
N,N′-diacetylchitobiose + H2O = N-acetyl-β-D-glucosaminyl-(1→4)-D-glucosamine + acetate |
Glossary: |
N,N′-diacetylchitobiose = N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine |
Other name(s): |
chitobiose amidohydolase; COD; chitin oligosaccharide deacetylase; chitin oligosaccharide amidohydolase; 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]-2-deoxy-D-glucopyranose acetylhydrolase |
Systematic name: |
N,N′-diacetylchitobiose acetylhydrolase |
Comments: |
Chitin oligosaccharide deacetylase is a key enzyme in the chitin catabolic cascade of chitinolytic Vibrio strains. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio parahemolyticus [2]. In contrast to EC 3.5.1.41 (chitin deacetylase) this enzyme is specific for the chitin disaccharide [1,3]. It also deacetylates the chitin trisaccharide with lower efficiency [3]. No activity with higher polymers of GlcNAc [1,3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kadokura, K., Rokutani, A., Yamamoto, M., Ikegami, T., Sugita, H., Itoi, S., Hakamata, W., Oku, T. and Nishio, T. Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin. Appl. Microbiol. Biotechnol. 75 (2007) 357–365. [DOI] [PMID: 17334758] |
2. |
Hirano, T., Kadokura, K., Ikegami, T., Shigeta, Y., Kumaki, Y., Hakamata, W., Oku, T. and Nishio, T. Heterodisaccharide 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a specific inducer of chitinolytic enzyme production in Vibrios harboring chitin oligosaccharide deacetylase genes. Glycobiology 19 (2009) 1046–1053. [DOI] [PMID: 19553519] |
3. |
Ohishi, K., Yamagishi, M., Ohta, T., Motosugi, M., Izumida, H., Sano, H., Adachi, K., Miwa, T. Purification and properties of two deacetylases produced by Vibrio alginolyticus H-8. Biosci. Biotechnol. Biochem. 61 (1997) 1113–1117. |
4. |
Ohishi, K., Murase, K., Ohta, T. and Etoh, H. Cloning and sequencing of the deacetylase gene from Vibrio alginolyticus H-8. J. Biosci. Bioeng. 90 (2000) 561–563. [DOI] [PMID: 16232910] |
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[EC 3.5.1.105 created 2010] |
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EC
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2.4.1.129
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Transferred entry: | peptidoglycan glycosyltransferase. Now EC 2.4.99.28, peptidoglycan glycosyltransferase
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[EC 2.4.1.129 created 1984, modified 2002, deleted 2023] |
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EC |
2.4.99.28 | Relevance: 73.7% |
Accepted name: |
peptidoglycan glycosyltransferase |
Reaction: |
[GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate |
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|
Glossary: |
Mur2Ac = N-acetylmuramic acid |
Other name(s): |
PG-II; bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase; penicillin binding protein (3 or 1B); peptidoglycan transglycosylase; undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase |
Systematic name: |
[poly-N-acetyl-D-glucosaminyl-(1→4)-(N-acetyl-D-muramoylpentapeptide)]-diphosphoundecaprenol:[N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide]-diphosphoundecaprenol disaccharidetransferase |
Comments: |
The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here). Involved in the synthesis of cell-wall peptidoglycan. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 79079-04-2 |
References: |
1. |
Taku, A., Stuckey, M. and Fan, D.P. Purification of the peptidoglycan transglycosylase of Bacillus megaterium. J. Biol. Chem. 257 (1982) 5018–5022. [DOI] [PMID: 6802846] |
2. |
Goffin, C. and Ghuysen, J.-M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62 (1998) 1079–1093. [DOI] [PMID: 9841666] |
3. |
van Heijenoort, J. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11 (2001) 25. [DOI] [PMID: 11320055] |
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[EC 2.4.99.28 created 1984 as EC 2.4.1.129, modified 2002, transferred 2023 to EC 2.4.99.28] |
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EC |
2.4.1.180 | Relevance: 71.1% |
Accepted name: |
lipopolysaccharide N-acetylmannosaminouronosyltransferase |
Reaction: |
UDP-N-acetyl-α-D-mannosaminouronate + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol |
Glossary: |
N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = lipid I = GlcNAc-pyrophosphorylundecaprenol = ditrans,octacis-undecaprenyl-N-acetyl-α-D-glucosaminyl diphosphate |
Other name(s): |
ManNAcA transferase; uridine diphosphoacetylmannosaminuronate-acetylglucosaminylpyrophosphorylundecaprenol acetylmannosaminuronosyltransferase; UDP-N-acetyl-β-D-mannosaminouronate:lipid I N-acetyl-β-D-mannosaminouronosyltransferase (incorrect) |
Systematic name: |
UDP-N-acetyl-α-D-mannosaminouronate:lipid I N-acetyl-α-D-mannosaminouronosyltransferase |
Comments: |
Involved in the biosynthesis of common antigen in Enterobacteriaceae. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 113478-30-1 |
References: |
1. |
Barr, K., Ward, S., Meier-Dieter, U., Mayer, H. and Rick, P.D. Characterization of an Escherichia coli rff mutant defective in transfer of N-acetylmannosaminuronic acid (ManNAcA) from UDP-ManNAcA to a lipid-linked intermediate involved in enterobacterial common antigen synthesis. J. Bacteriol. 170 (1988) 228–233. [DOI] [PMID: 3275612] |
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[EC 2.4.1.180 created 1990, modified 2011] |
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EC |
3.2.1.149 | Relevance: 70% |
Accepted name: |
β-primeverosidase |
Reaction: |
a 6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside + H2O = 6-O-(β-D-xylopyranosyl)-β-D-glucopyranose + an alcohol |
Glossary: |
primeverose = 6-O-(β-D-xylopyranosyl)-D-glucose
vicianose = 6-O-(α-L-arabinopyranosyl)-D-glucose |
Systematic name: |
6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside 6-O-(β-D-xylosyl)-β-D-glucohydrolase |
Comments: |
The enzyme is responsible for the formation of the alcoholic aroma in oolong and black tea. In addition to β-primeverosides [i.e. 6-O-(β-D-xylopyranosyl)-β-D-glucopyranosides], it also hydrolyses 6-O-(β-D-apiofuranosyl)-β-D-glucopyranosides and, less rapidly, β-vicianosides and 6-O-(α-L-arabinofuranosyl)-β-D-glucopyranosides, but not β-glucosides. Geranyl-, linaloyl-, benzyl- and p-nitrophenol glycosides are all hydrolysed. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 884593-92-4 |
References: |
1. |
Ijima, Y., Ogawa, K., Watanabe, N., Usui, T., Ohnishi-Kameyama, M., Nagata, T. and Sakata, K. Characterization of β-primeverosidase, being concerned with alcoholic aroma formation in tea leaves to be processed into black tea, and preliminary observations on its substrate specificity. J. Agric. Food Chem. 46 (1998) 1712–1718. |
2. |
Ogawa, K., Ijima, Y., Guo, W., Watanabe, N., Usui, T., Dong, S., Tong, Q. and Sakata, K. Purification of a β-primeverosidase concerned with alcoholic aroma formation in tea leaves (cv. Shuxian) to be processed to oolong tea. J. Agric. Food Chem. 45 (1997) 877–882. |
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[EC 3.2.1.149 created 2001] |
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EC |
5.1.3.26 | Relevance: 68.3% |
Accepted name: |
N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase |
Reaction: |
N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = N-acetyl-α-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol |
Other name(s): |
GlcNAc-P-P-Und epimerase; GlcNAc-P-P-Und 4-epimerase; gne (gene name) |
Systematic name: |
N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase |
Comments: |
The enzyme is involved in biosynthesis of the repeating tetrasaccharide unit of the O-antigen produced by some Gram-negative bacteria. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Rush, J.S., Alaimo, C., Robbiani, R., Wacker, M. and Waechter, C.J. A novel epimerase that converts GlcNAc-P-P-undecaprenol to GalNAc-P-P-undecaprenol in Escherichia coli O157. J. Biol. Chem. 285 (2010) 1671–1680. [DOI] [PMID: 19923219] |
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[EC 5.1.3.26 created 2013] |
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EC |
3.2.1.21 | Relevance: 67.8% |
Accepted name: |
β-glucosidase |
Reaction: |
Hydrolysis of terminal, non-reducing β-D-glucosyl residues with release of β-D-glucose |
Other name(s): |
gentiobiase; cellobiase; emulsin; elaterase; aryl-β-glucosidase; β-D-glucosidase; β-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl β-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; β-1,6-glucosidase |
Systematic name: |
β-D-glucoside glucohydrolase |
Comments: |
Wide specificity for β-D-glucosides. Some examples also hydrolyse one or more of the following: β-D-galactosides, α-L-arabinosides, β-D-xylosides, β-D-fucosides. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-22-3 |
References: |
1. |
Chinchetru, M.A., Cabezas, J.A. and Calvo, P. Purification and characterization of a broad specificity β-glucosidase from sheep liver. Int. J. Biochem. 21 (1989) 469–476. [PMID: 2503402] |
2. |
Conchie, J. β-Glucosidase from rumen liquor. Preparation, assay and kinetics of action. Biochem. J. 58 (1954) 552–560. [PMID: 13230003] |
3. |
Dahlqvist, A. Pig intestinal β-glucosidase activities. I. Relation to β-galactosidase (lactase). Biochim. Biophys. Acta 50 (1961) 55–61. [DOI] [PMID: 13719334] |
4. |
Heyworth, R. and Walker, P.G. Almond-emulsin β-D-glucosidase and β-D-galactosidase. Biochem. J. 83 (1962) 331–335. [PMID: 13907157] |
5. |
Larner, J. Other glucosidases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 369–378. |
6. |
Sano, K., Amemura, A. and Harada, T. Purification and properties of a β-1,6-glucosidase from Flavobacterium. Biochim. Biophys. Acta 377 (1975) 410–420. [DOI] [PMID: 235305] |
|
[EC 3.2.1.21 created 1961] |
|
|
|
|
EC |
2.5.1.98 | Relevance: 66.9% |
Accepted name: |
Rhizobium leguminosarum exopolysaccharide glucosyl ketal-pyruvate-transferase |
Reaction: |
phosphoenolpyruvate + [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n = [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO-)C-β-D-Gal-(1→3)-4,6-CH3(COO-)C-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n + phosphate
|
Other name(s): |
PssM; phosphoenolpyruvate:[D-GlcA-β-(1→4)-2-O-Ac-D-GlcA-β-(1→4)-D-Glc-β-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-D-Gal-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→6)]-2(or 3)-O-Ac-D-Glc-α-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase |
Systematic name: |
phosphoenolpyruvate:[β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-4,6-CH3(COO-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase |
Comments: |
The enzyme is responsible for pyruvylation of the subterminal glucose in the acidic octasaccharide repeating unit of the exopolysaccharide of Rhizobium leguminosarum (bv. viciae strain VF39) which is necessary to establish nitrogen-fixing symbiosis with Pisum sativum, Vicia faba, and Vicia sativa. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ivashina, T.V., Fedorova, E.E., Ashina, N.P., Kalinchuk, N.A., Druzhinina, T.N., Shashkov, A.S., Shibaev, V.N. and Ksenzenko, V.N. Mutation in the pssM gene encoding ketal pyruvate transferase leads to disruption of Rhizobium leguminosarum bv. viciae—Pisum sativum symbiosis. J. Appl. Microbiol. 109 (2010) 731–742. [DOI] [PMID: 20233262] |
|
[EC 2.5.1.98 created 2012, modified 2018] |
|
|
|
|
EC |
3.2.1.6 | Relevance: 66.2% |
Accepted name: |
endo-1,3(4)-β-glucanase |
Reaction: |
Endohydrolysis of (1→3)- or (1→4)-linkages in β-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3 |
Other name(s): |
endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3(4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1→3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-β-(1-3)-D-glucanase; endo-β-1,3-glucanase IV; endo-1,3-β-D-glucanase; 1,3-(1,3;1,4)-β-D-glucan 3(4)-glucanohydrolase |
Systematic name: |
3(or 4)-β-D-glucan 3(4)-glucanohydrolase |
Comments: |
Substrates include laminarin, lichenin and cereal D-glucans; different from EC 3.2.1.52 β-N-acetylhexosaminidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-14-3 |
References: |
1. |
Barras, D.R. and Stone, B.A. β-1,3-Glucan hydrolases from Euglena gracilis. I. The nature of the hydrolases. Biochim. Biophys. Acta 191 (1969) 329–341. [DOI] [PMID: 5354264] |
2. |
Barras, D.R. and Stone, B.A. β-1,3-Glucan hydrolases from Euglena gracilis. II. Purification and properties of the β-1,3-glucan exo-hydrolase. Biochim. Biophys. Acta 191 (1969) 342–353. [DOI] [PMID: 5354265] |
3. |
Cunningham, L.W. and Manners, D.J. Enzymic degradation of lichenin. Biochem. J. 80 (1961) 42. |
4. |
Reese, E.T. and Mandels, M. β-D-1,3-Glucanases in fungi. Can. J. Microbiol. 5 (1959) 173–185. [PMID: 13638895] |
5. |
Sova, V.V., Elyakova, L.A. and Vaskovsky, V.E. Purification and some properties of β-1,3-glucan glucanohydrolase from the crystalline style of bivalvia, Spisula sachalinensis. Biochim. Biophys. Acta 212 (1970) 111–115. [DOI] [PMID: 5500926] |
|
[EC 3.2.1.6 created 1961, modified 1976] |
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|
|
|
EC |
3.5.1.89 | Relevance: 65.9% |
Accepted name: |
N-acetylglucosaminylphosphatidylinositol deacetylase |
Reaction: |
6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate |
|
For diagram of glycosylphosphatidyl-myo-inositol biosynthesis, click here |
Other name(s): |
N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase; N-acetylglucosaminylphosphatidylinositol de-N-acetylase; GlcNAc-PI de-N-acetylase; GlcNAc-PI deacetylase; acetylglucosaminylphosphatidylinositol deacetylase |
Systematic name: |
6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol acetylhydrolase |
Comments: |
Involved in the second step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. The enzyme appears to be composed of a single subunit (PIG-L in mammalian cells and GPI12 in yeast). In some species, the long-chain sn-1-acyl group of the phosphatidyl group is replaced by a long-chain alkyl or alk-1-enyl group. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122191-30-4 |
References: |
1. |
Doering, T.L., Masteron, W.J., Englund, P.T. and Hart, G.W. Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine. J. Biol. Chem. 264 (1989) 11168–11173. [PMID: 2525555] |
2. |
Nakamura, N., Inoue, N., Watanabe, R., Takahashi, M., Takeda, J., Stevens, V.L. and Kinoshita, T. Expression cloning of PIG-L, a candidate N-acetylglucosaminyl-phosphatidylinositol deacetylase. J. Biol. Chem. 272 (1997) 15834–15840. [DOI] [PMID: 9188481] |
3. |
Watanabe, R., Ohishi, K., Maeda, Y., Nakamura, N. and Kinoshita, T. Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem. J. 339 (1999) 185–192. [PMID: 10085243] |
4. |
Smith, T.K, Crossman, A., Borissow, C.N., Paterson, M.J., Dix, A., Brimacombe, J.S. and Ferguson, M.A.J. Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors. EMBO J. 20 (2001) 3322–3332. [DOI] [PMID: 11432820] |
|
[EC 3.5.1.89 created 1992 as EC 3.1.1.69, transferred 2002 to EC 3.5.1.89, modified 2002] |
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|
EC |
3.2.1.187 | Relevance: 65.5% |
Accepted name: |
(Ara-f)3-Hyp β-L-arabinobiosidase |
Reaction: |
4-O-(β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + H2O = 4-O-(β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranose |
Glossary: |
4-O-(β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline = (Ara-f)3-Hyp |
Other name(s): |
hypBA2 (gene name); β-L-arabinobiosidase |
Systematic name: |
4-O-(β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranose hydrolase |
Comments: |
The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, is specific for (Ara-f)3-Hyp, a sugar chain found in hydroxyproline-rich glyoproteins such as extensin and lectin. The enzyme was not able to accept (Ara-f)2-Hyp or (Ara-f)4-Hyp as substrates. In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Fujita, K., Sakamoto, S., Ono, Y., Wakao, M., Suda, Y., Kitahara, K. and Suganuma, T. Molecular cloning and characterization of a β-L-Arabinobiosidase in Bifidobacterium longum that belongs to a novel glycoside hydrolase family. J. Biol. Chem. 286 (2011) 5143–5150. [DOI] [PMID: 21149454] |
|
[EC 3.2.1.187 created 2013] |
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|
EC |
3.2.1.52 | Relevance: 65.2% |
Accepted name: |
β-N-acetylhexosaminidase |
Reaction: |
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-β-D-hexosaminides |
Other name(s): |
hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-β-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhexosaminidase; β-N-acetyl-D-hexosaminidase; β-N-acetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase; β-D-hexosaminidase; NAHase |
Systematic name: |
β-N-acetyl-D-hexosaminide N-acetylhexosaminohydrolase |
Comments: |
Acts on N-acetylglucosides and N-acetylgalactosides. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-33-3 |
References: |
1. |
Cabezas, J.A. Some comments on the type references of the official nomenclature (IUB) for β-N-acetylglucosaminidase, β-N-acetylhexosaminidase and β-N-acetylgalactosaminidase. Biochem. J. 261 (1989) 1059–1060. [PMID: 2529847] |
2. |
Calvo, P., Reglero, A. and Cabezas, J.A. Purification and properties of β-N-acetylhexosaminidase from the mollusc Helicella ericetorum Muller. Biochem. J. 175 (1978) 743–750. [PMID: 33660] |
3. |
Frohwein, Y.S. and Gatt, S. Isolation of β-N-acetylhexosaminidase, β-N-acetylglucosaminidase, and β-N-acetylgalactosaminidase from calf brain. Biochemistry 6 (1967) 2775–2782. [PMID: 6055190] |
4. |
Li, S.-C. and Li, Y.-T. Studies on the glycosidases of jack bean meal. 3. Crystallization and properties of β-N-acetylhexosaminidase. J. Biol. Chem. 245 (1970) 5153–5160. [PMID: 5506280] |
|
[EC 3.2.1.52 created 1972 (EC 3.2.1.30 created 1961, incorporated 1992 [EC 3.2.1.29 created 1961, incorporated 1972])] |
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|
|
EC |
2.4.1.226 | Relevance: 65.1% |
Accepted name: |
N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase |
Reaction: |
(1) UDP-α-D-glucuronate + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine (2) UDP-α-D-glucuronate + [protein]-3-O-([β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-[β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine |
|
For diagram of chondroitin biosynthesis (later stages), click here |
Other name(s): |
chondroitin glucuronyltransferase II; α-D-glucuronate:N-acetyl-β-D-galactosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 3-β-glucuronosyltransferase; UDP-α-D-glucuronate:N-acetyl-β-D-galactosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 3-β-glucuronosyltransferase |
Systematic name: |
UDP-α-D-glucuronate:[protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 3-β-glucuronosyltransferase (configuration-inverting) |
Comments: |
Involved in the biosynthesis of chondroitin and dermatan sulfate. The human chondroitin synthetase is a bifunctional glycosyltransferase, which has the 3-β-glucuronosyltransferase and 4-β-N-acetylgalactosaminyltransferase (EC 2.4.1.175) activities required for the synthesis of the chondroitin sulfate disaccharide repeats. Similar chondroitin synthase ’co-polymerases’ can be found in Pasteurella multocida and Escherichia coli. There is also another human protein with apparently only the 3-β-glucuronosyltransferase activity. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 269077-98-7 |
References: |
1. |
Kitagawa, H., Uyama, T. and Sugahara, K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721–38726. [DOI] [PMID: 11514575] |
2. |
DeAngelis, P.L. and Padgett-McCue, A.J. Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F. J. Biol. Chem. 275 (2000) 24124–24129. [DOI] [PMID: 10818104] |
3. |
Ninomiya, T., Sugiura, N., Tawada, A., Sugimoto, K., Watanabe, H. and Kimata, K. Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4. J. Biol. Chem. 277 (2002) 21567–21575. [DOI] [PMID: 11943778] |
4. |
Gotoh, M., Yada, T., Sato, T., Akashima, T., Iwasaki, H., Mochizuki, H., Inaba, N., Togayachi, A., Kudo, T., Watanabe, H., Kimata, K. and Narimatsu, H. Molecular cloning and characterization of a novel chondroitin sulfate glucuronyltransferase which transfers glucuronic acid to N-acetylgalactosamine. J. Biol. Chem. 277 (2002) 38179–38188. [DOI] [PMID: 12145278] |
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[EC 2.4.1.226 created 2002, modified 2018] |
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|
EC |
3.5.2.6 | Relevance: 65% |
Accepted name: |
β-lactamase |
Reaction: |
a β-lactam + H2O = a substituted β-amino acid |
|
For diagram of penicillin biosynthesis and metabolism, click here |
Other name(s): |
penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I; penicillinase II; β-lactamase I; β-lactamase II; β-lactamase III; β-lactamase A; β-lactamase B; β-lactamase C; β-lactamase AME I; cephalosporin-β-lactamase; carbapenemase |
Systematic name: |
β-lactam hydrolase |
Comments: |
A group of enzymes of varying specificity hydrolysing β-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9073-60-3 |
References: |
1. |
Citri, N. Penicillinase and other β-lactamases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 4, Academic Press, New York, 1971, pp. 23–46. |
2. |
Hennessey, T.D. and Richmond, M.H. The purification and some properties of a β-lactamase (cephalosporinase) synthesized by Enterobacter cloacae. Biochem. J. 109 (1968) 469–473. [PMID: 5685878] |
3. |
Kuwabara, S. Purification and properties of two extracellular β-lactamases from Bacillus cereus 569-H. Biochem. J. 118 (1970) 457–465. [PMID: 4990588] |
4. |
Pollock, M.R. Penicillinase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 269–278. |
5. |
Pollock, M.R., Torriani, A.-M. and Tridgell, E.G. Crystalline bacterial penicillinase. Biochem. J. 62 (1956) 387–391. [PMID: 13303985] |
6. |
Ross, G.W. and Boulton, M.G. Purification of β-lactamases on QAE-sephadex. Biochim. Biophys. Acta 309 (1973) 430–439. [DOI] [PMID: 4731970] |
|
[EC 3.5.2.6 created 1961, modified 1981 (EC 3.5.2.8 created 1972, incorporated 1978)] |
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|
|
|
EC |
3.2.1.74 | Relevance: 64.9% |
Accepted name: |
glucan 1,4-β-glucosidase |
Reaction: |
Hydrolysis of (1→4)-linkages in (1→4)-β-D-glucans, to remove successive glucose units |
Other name(s): |
exo-1,4-β-glucosidase; exocellulase; exo-β-1,4-glucosidase; exo-β-1,4-glucanase; β-1,4-β-glucanase; β-glucosidase; exo-1,4-β-glucanase; 1,4-β-D-glucan glucohydrolase |
Systematic name: |
4-β-D-glucan glucohydrolase |
Comments: |
Acts on 1,4-β-D-glucans and related oligosaccharides. Cellobiose is hydrolysed, but very slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-52-1 |
References: |
1. |
Barras, D.R., Moore, A.E. and Stone, B.A. Enzyme-substrate relations among β-glucan hydrolases. Adv. Chem. Ser. 95 (1969) 105–138. |
|
[EC 3.2.1.74 created 1972] |
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|
|
|
EC |
3.2.1.37 | Relevance: 64.4% |
Accepted name: |
xylan 1,4-β-xylosidase |
Reaction: |
Hydrolysis of (1→4)-β-D-xylans, to remove successive D-xylose residues from the non-reducing termini |
Other name(s): |
xylobiase; β-xylosidase; exo-1,4-β-xylosidase; β-D-xylopyranosidase; β-xylosidase; β-xylosidase; exo-1,4-xylosidase; exo-1,4-β-D-xylosidase; 1,4-β-D-xylan xylohydrolase |
Systematic name: |
4-β-D-xylan xylohydrolase |
Comments: |
Also hydrolyses xylobiose. Some other exoglycosidase activities have been found associated with this enzyme in sheep liver. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-53-0 |
References: |
1. |
Chinchetru, M.A., Cabezas, J.A. and Calvo, P. Purification and characterization of a broad specificity β-glucosidase from sheep liver. Int. J. Biochem. 21 (1989) 469–476. [PMID: 2503402] |
2. |
Howard, B.H., Jones, G. and Purdom, M.R. The pentosanases of some rumen bacteria. Biochem. J. 74 (1960) 173–180. [PMID: 14403433] |
|
[EC 3.2.1.37 created 1965] |
|
|
|
|
EC |
3.2.1.75 | Relevance: 64.3% |
Accepted name: |
glucan endo-1,6-β-glucosidase |
Reaction: |
Random hydrolysis of (1→6)-linkages in (1→6)-β-D-glucans |
Other name(s): |
endo-1,6-β-glucanase; β-1→6)-β-D-glucanase; β-1,6-glucanase-pustulanase; β-1,6-glucan hydrolase; β-1,6-glucan 6-glucanohydrolase; 1,6-β-D-glucan glucanohydrolase |
Systematic name: |
6-β-D-glucan glucanohydrolase |
Comments: |
Acts on lutean, pustulan and 1,6-oligo-β-D-glucosides. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-39-0 |
References: |
1. |
Reese, E.T., Parrish, F.W. and Mandels, M. β-D-1,6-Glucanases in fungi. Can. J. Microbiol. 8 (1962) 327–334. [PMID: 14491003] |
|
[EC 3.2.1.75 created 1972] |
|
|
|
|
EC |
3.2.1.38 | Relevance: 63.7% |
Accepted name: |
β-D-fucosidase |
Reaction: |
Hydrolysis of terminal non-reducing β-D-fucose residues in β-D-fucosides |
Other name(s): |
β-fucosidase |
Systematic name: |
β-D-fucoside fucohydrolase |
Comments: |
Enzymes from some sources also hydrolyse β-D-galactosides and/or β-D-glucosides and/or α-L-arabinosides. The activity of EC 3.2.1.37 xylan 1,4-β-xylosidase, is an associated activity found in some sources (e.g. liver). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-34-7 |
References: |
1. |
Chinchetru, M.A., Cabezas, J.A. and Calvo, P. Characterization and kinetics of β-D-gluco/fuco/galactosidase from sheep liver. Comp. Biochem. Physiol. B 75 (1983) 719–728. [PMID: 6413126] |
2. |
Chinchetru, M.A., Cabezas, J.A. and Calvo, P. Purification and characterization of a broad specificity β-glucosidase from sheep liver. Int. J. Biochem. 21 (1989) 469–476. [PMID: 2503402] |
3. |
Rodriguez, J.A., Cabezas, J.A. and Calvo, P. β-Fucosidase, β-glucosidase and β-galactosidase activities associated in bovine liver. Int. J. Biochem. 14 (1982) 695–698. [PMID: 6811346] |
4. |
Wiederschain, G. and Prokopenkov, A. β-D-Galactosidase and β-D-fucosidase of pig kidney. Arch. Biochem. Biophys. 158 (1973) 539–543. [DOI] [PMID: 4782520] |
5. |
Wiederschain, G.Y., Beyer, E.M., Klyaschitsty, B.A. and Shashkov, A.S. Specificity patterns of different types of human fucosidase. Recognition of a certain region of the pyranose ring in sugars by the enzymes. Biochim. Biophys. Acta 659 (1981) 434–444. [DOI] [PMID: 6789883] |
|
[EC 3.2.1.38 created 1965, deleted 1972, reinstated 1978] |
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|
EC |
2.7.8.15 | Relevance: 63.3% |
Accepted name: |
UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphosphodolichol |
|
For diagram of dolichyltetradecasaccharide biosynthesis, click here |
Other name(s): |
UDP-D-N-acetylglucosamine N-acetylglucosamine 1-phosphate transferase; UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase; UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase; uridine diphosphoacetylglucosamine-dolichyl phosphate acetylglucosamine-1-phosphotransferase; chitobiosylpyrophosphoryldolichol synthase; dolichol phosphate N-acetylglucosamine-1-phosphotransferase; UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase; UDP-acetylglucosamine-dolichol phosphate acetylglucosamine-1-phosphotransferase |
Systematic name: |
UDP-N-α-acetyl-D-glucosamine:dolichyl-phosphate N-acetyl-D-glucosaminephosphotransferase (configuration-retaining) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 70431-08-2 |
References: |
1. |
Sharma, C.B., Lehle, L. and Tanner, W. Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast. Eur. J. Biochem. 126 (1982) 319–325. [DOI] [PMID: 6215245] |
2. |
Villemez, C.L. and Carlo, P.L. Properties of a soluble polyprenyl phosphate. UDP-D-N-acetylglucosamine N-acetylglucosamine-1-phosphate transferase. J. Biol. Chem. 255 (1980) 8174–8178. [PMID: 6447695] |
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[EC 2.7.8.15 created 1983] |
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EC |
3.2.1.23 | Relevance: 62.8% |
Accepted name: |
β-galactosidase |
Reaction: |
Hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides |
Other name(s): |
lactase (ambiguous); β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat |
Systematic name: |
β-D-galactoside galactohydrolase |
Comments: |
Some enzymes in this group hydrolyse α-L-arabinosides; some animal enzymes also hydrolyse β-D-fucosides and β-D-glucosides; cf. EC 3.2.1.108 lactase. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9031-11-2 |
References: |
1. |
Blakely, J.A. and MacKenzie, S.L. Purification and properties of a β-hexosidase from Sporobolomyces singularis. Can. J. Biochem. 47 (1969) 1021–1025. [PMID: 5389663] |
2. |
Kuby, S.A. and Lardy, H.A. Purification and kinetics of β-D-galactosidase from Escherichia coli, strain K-12. J. Am. Chem. Soc. 75 (1953) 890–896. |
3. |
Kuo, C.H. and Wells, W.W. β-Galactosidase from rat mammary gland. Its purification, properties, and role in the biosynthesis of 6β-O-D-galactopyranosyl myo-inositol. J. Biol. Chem. 253 (1978) 3550–3556. [PMID: 418065] |
4. |
Landman, O.E. Properties and induction of β-galactosidase in Bacillus megaterium. Biochim. Biophys. Acta 23 (1957) 558–569. [PMID: 13426167] |
5. |
Llanillo, M., Perez, N. and Cabezas, J.A. β-Galactosidase and β-glucosidase activities of the same enzyme from rabbit liver. Int. J. Biochem. 8 (1977) 557–564. |
6. |
Monod, J. and Cohn, M. La biosynthèse induite des enzymes (adaptation enzymatique). Adv. Enzymol. Relat. Subj. Biochem. 13 (1952) 67–119. [PMID: 14943665] |
7. |
Wallenfels, K. and Malhotra, O.P. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 409–430. |
8. |
Asp, N.G., Dahlqvist, A. and Koldovský, O. Human small-intestinal β-galactosidases. Separation and characterization of one lactase and one hetero β-galactosidase. Biochem. J. 114 (1969) 351–359. [PMID: 5822067] |
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[EC 3.2.1.23 created 1961, modified 1980] |
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EC |
2.4.1.135 | Relevance: 62.8% |
Accepted name: |
galactosylgalactosylxylosylprotein 3-β-glucuronosyltransferase |
Reaction: |
UDP-α-D-glucuronate + [protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine |
|
For diagram of heparan and chondroitin biosynthesis (early stages), click here |
Glossary: |
[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = [protein]-3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine |
Other name(s): |
glucuronosyltransferase I; uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase; UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosyl-protein D-glucuronosyltransferase; UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein D-glucuronosyltransferase |
Systematic name: |
UDP-α-D-glucuronate:[protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine D-glucuronosyltransferase (configuration-inverting) |
Comments: |
Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 227184-75-0 |
References: |
1. |
Helting, J. and Roden, L. Biosynthesis of chondroitin sulfate. II. Glucuronosyl transfer in the formation of the carbohydrate-protein linkage region. J. Biol. Chem. 244 (1969) 2799–2805. [PMID: 5770003] |
2. |
Helting, T. Biosynthesis of heparin. Solubilization and partial purification of uridine diphosphate glucuronic acid: acceptor glucuronosyltransferase from mouse mastocytoma. J. Biol. Chem. 247 (1972) 4327–4332. [PMID: 4260846] |
3. |
Kitagawa, H., Tone, Y., Tamura, J., Neumann, K.W., Ogawa, T., Oka, S., Kawasaki, T. and Sugahara, K. Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 273 (1998) 6615–6618. [DOI] [PMID: 9506957] |
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[EC 2.4.1.135 created 1984, modified 2002, modified 2016] |
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EC |
2.4.1.174 | Relevance: 62.6% |
Accepted name: |
glucuronylgalactosylproteoglycan 4-β-N-acetylgalactosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-galactosamine + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine |
|
For diagram of chondroitin biosynthesis (later stages), click here |
Glossary: |
[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = [protein]-3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine |
Other name(s): |
N-acetylgalactosaminyltransferase I; glucuronylgalactosylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I; UDP-N-acetyl-D-galactosamine:D-glucuronyl-1,3-β-D-galactosyl-proteoglycan β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:D-glucuronyl-(1→3)-β-D-galactosyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase |
Systematic name: |
UDP-N-acetyl-D-galactosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4-β-N-acetylgalactosaminyltransferase (configuration-inverting) |
Comments: |
Requires Mn2+. Involved in the biosynthesis of chondroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 96189-39-8 |
References: |
1. |
Rohrmann, K., Niemann, R. and Buddecke, E. Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate. Eur. J. Biochem. 148 (1985) 463–469. [DOI] [PMID: 3922754] |
2. |
Uyama, T., Kitagawa, H., Tamura, J.-i. and Sugahara, K. Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: the key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate. J. Biol. Chem. 277 (2002) 8841–8846. [DOI] [PMID: 11788602] |
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[EC 2.4.1.174 created 1989, modified 2002] |
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EC |
3.2.1.39 | Relevance: 62.3% |
Accepted name: |
glucan endo-1,3-β-D-glucosidase |
Reaction: |
Hydrolysis of (1→3)-β-D-glucosidic linkages in (1→3)-β-D-glucans |
Other name(s): |
endo-1,3-β-glucanase; laminarinase; laminaranase; oligo-1,3-glucosidase; endo-1,3-β-glucanase; callase; β-1,3-glucanase; kitalase; 1,3-β-D-glucan 3-glucanohydrolase; endo-(1,3)-β-D-glucanase; (1→3)-β-glucan 3-glucanohydrolase; endo-1,3-β-D-glucanase; endo-1,3-β-glucosidase; 1,3-β-D-glucan glucanohydrolase |
Systematic name: |
3-β-D-glucan glucanohydrolase |
Comments: |
Different from EC 3.2.1.6 endo-1,3(4)-β-glucanase. Very limited action on mixed-link (1→3,1→4)-β-D-glucans. Hydrolyses laminarin, paramylon and pachyman. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-37-0 |
References: |
1. |
Chesters, C.G.C. and Bull, A.T. The enzymic degradation of laminarin. 2. The multicomponent nature of fungal laminarinases. Biochem. J. 86 (1963) 31–38. [PMID: 14020682] |
2. |
Reese, E.T. and Mandels, M. β-D-1,3-Glucanases in fungi. Can. J. Microbiol. 5 (1959) 173–185. [PMID: 13638895] |
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[EC 3.2.1.39 created 1965] |
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EC |
3.2.1.213 | Relevance: 62.2% |
Accepted name: |
galactan exo-1,6-β-galactobiohydrolase (non-reducing end) |
Reaction: |
Hydrolysis of (1→6)-β-D-galactosidic linkages in arabinogalactan proteins and (1→3):(1→6)-β-galactans to yield (1→6)-β-galactobiose as the final product. |
Other name(s): |
exo-β-1,6-galactobiohydrolase; 1,6Gal (gene name) |
Systematic name: |
exo-β-(1→6)-galactobiohydrolase (non-reducing end) |
Comments: |
The enzyme, characterized from the bacterium Bifidobacterium longum, specifically hydrolyses (1→6)-β-galactobiose from the non-reducing terminal of (1→6)-β-D-galactooligosaccharides with a degree of polymerization (DP) of 3 or higher, using an exo mode of action. The enzyme cannot hydrolyse α-L-arabinofuranosylated (1→6)-β-galactans (as found in arabinogalactans) and does not act on (1→3)-β-D- or (1→4)-β-D-galactans. cf. EC 3.2.1.164, galactan endo-1,6-β-galactosidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Fujita, K., Sakamoto, A., Kaneko, S., Kotake, T., Tsumuraya, Y. and Kitahara, K. Degradative enzymes for type II arabinogalactan side chains in Bifidobacterium longum subsp. longum. Appl. Microbiol. Biotechnol. 103 (2019) 1299–1310. [PMID: 30564851] |
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[EC 3.2.1.213 created 2020] |
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EC |
3.4.11.25 | Relevance: 62.1% |
Accepted name: |
β-peptidyl aminopeptidase |
Reaction: |
Cleaves N-terminal β-homoamino acids from peptides composed of 2 to 6 amino acids |
Other name(s): |
BapA (ambiguous) |
Comments: |
Sphingosinicella xenopeptidilytica strain 3-2W4 is able to utilize the β-peptides β-homoVal-β-homoAla-β-homoLeu and β-homoAla-β-homoLeu as sole carbon and energy sources [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB |
References: |
1. |
Heck, T., Limbach, M., Geueke, B., Zacharias, M., Gardiner, J., Kohler, H.P. and Seebach, D. Enzymatic degradation of β- and mixed α,β-oligopeptides. Chem. Biodivers. 3 (2006) 1325–1348. [DOI] [PMID: 17193247] |
2. |
Geueke, B., Namoto, K., Seebach, D. and Kohler, H.P. A novel β-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves
peptide bonds of synthetic β-tri- and β-dipeptides. J. Bacteriol. 187 (2005) 5910–5917. [DOI] [PMID: 16109932] |
3. |
Geueke, B., Heck, T., Limbach, M., Nesatyy, V., Seebach, D. and Kohler, H.P. Bacterial β-peptidyl aminopeptidases with unique substrate specificities for β-oligopeptides and mixed β,α-oligopeptides. FEBS J. 273 (2006) 5261–5272. [DOI] [PMID: 17064315] |
4. |
Heck, T., Kohler, H.P., Limbach, M., Flögel, O., Seebach, D. and Geueke, B. Enzyme-catalyzed formation of β-peptides: β-peptidyl aminopeptidases BapA and DmpA acting as β-peptide-synthesizing enzymes. Chem. Biodivers. 4 (2007) 2016. [DOI] [PMID: 17886858] |
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[EC 3.4.11.25 created 2011] |
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EC |
3.2.1.161 | Relevance: 62% |
Accepted name: |
β-apiosyl-β-glucosidase |
Reaction: |
7-[β-D-apiofuranosyl-(1→6)-β-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + β-D-apiofuranosyl-(1→6)-D-glucose |
Other name(s): |
isoflavonoid-7-O-β[D-apiosyl-(1→6)-β-D-glucoside] disaccharidase; isoflavonoid 7-O-β-apiosyl-glucoside β-glucosidase; furcatin hydrolase |
Systematic name: |
7-[β-D-apiofuranosyl-(1→6)-β-D-glucopyranosyloxy]isoflavonoid β-D-apiofuranosyl-(1→6)-D-glucohydrolase |
Comments: |
The enzyme from the tropical tree Dalbergia nigrescens Kurz belongs in glycosyl hydrolase family 1. The enzyme removes disaccharides from the natural substrates dalpatein 7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside and 7-hydroxy-2′,4′,5′,6-tetramethoxy-7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside (dalnigrein 7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside) although it can also remove a single glucose residue from isoflavonoid 7-O-glucosides [2]. Daidzin and genistin are also substrates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 1000598-83-3 |
References: |
1. |
Hosel, W. and Barz, W. β-Glucosidases from Cicer arietinum L. Purification and Properties of
isoflavone-7-O-glucoside-specific β-glucosidases. Eur. J. Biochem. 57 (1975) 607–616. [DOI] [PMID: 240725] |
2. |
Chuankhayan, P., Hua, Y., Svasti, J., Sakdarat, S., Sullivan, P.A. and Ketudat Cairns, J.R. Purification of an isoflavonoid 7-O-β-apiosyl-glucoside
β-glycosidase and its substrates from Dalbergia nigrescens Kurz. Phytochemistry 66 (2005) 1880–1889. [DOI] [PMID: 16098548] |
3. |
Ahn, Y.O., Mizutani, M., Saino, H. and Sakata, K. Furcatin hydrolase from Viburnum furcatum Blume is a novel
disaccharide-specific acuminosidase in glycosyl hydrolase family 1. J. Biol. Chem. 279 (2004) 23405–23414. [DOI] [PMID: 14976214] |
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[EC 3.2.1.161 created 2006] |
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EC |
2.4.1.175 | Relevance: 61.5% |
Accepted name: |
glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase |
Reaction: |
(1) UDP-N-acetyl-α-D-galactosamine + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine (2) UDP-N-acetyl-α-D-galactosamine + [protein]-3-O-(β-D-GlcA-(1→3)-[β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-([β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n+1-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine |
|
For diagram of chondroitin biosynthesis (later stages), click here |
Other name(s): |
N-acetylgalactosaminyltransferase II; UDP-N-acetyl-D-galactosamine:D-glucuronyl-N-acetyl-1,3-β-D-galactosaminylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; chondroitin synthase; glucuronyl-N-acetylgalactosaminylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase II; UDP-N-acetyl-D-galactosamine:β-D-glucuronosyl-(1→3)-N-acetyl-β-D-galactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase; UDP-N-acetyl-α-D-galactosamine:β-D-glucuronosyl-(1→3)-N-acetyl-β-D-galactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-galactosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4-β-N-acetylgalactosaminyltransferase (configuration-inverting) |
Comments: |
Involved in the biosynthesis of chondroitin sulfate. The human form of this enzyme is a bifunctional glycosyltransferase, which also has the 3-β-glucuronosyltransferase (EC 2.4.1.226, N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase) activity required for the synthesis of the chondroitin sulfate disaccharide repeats. Similar chondroitin synthase ’co-polymerases’ can be found in Pasteurella multocida and Escherichia coli. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 96189-40-1 |
References: |
1. |
Rohrmann, K., Niemann, R. and Buddecke, E. Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate. Eur. J. Biochem. 148 (1985) 463–469. [DOI] [PMID: 3922754] |
2. |
Kitagawa, H., Uyama, T. and Sugahara, K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721–38726. [DOI] [PMID: 11514575] |
3. |
DeAngelis, P.L. and Padgett-McCue, A.J. Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F. J. Biol. Chem. 275 (2000) 24124–24129. [DOI] [PMID: 10818104] |
4. |
Ninomiya, T., Sugiura, N., Tawada, A., Sugimoto, K., Watanabe, H. and Kimata, K. Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4. J. Biol. Chem. 277 (2002) 21567–21575. [DOI] [PMID: 11943778] |
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[EC 2.4.1.175 created 1989, modified 2002] |
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EC |
2.3.1.213 | Relevance: 61.1% |
Accepted name: |
cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) 6′′′-O-hydroxycinnamoyltransferase |
Reaction: |
1-O-(4-hydroxycinnamoyl)-β-D-glucose + cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) = β-D-glucose + cyanidin 3-O-[6-O-(6-O-4-hydroxycinnamoyl-β-D-glucosyl)-2-O-β-D-xylosyl-β-D-galactoside] |
|
For diagram of cyanidin galactoside biosynthesis, click here |
Glossary: |
1-O-(4-hydroxycinnamoyl)-β-D-glucose = 1-O-(4-coumaroyl)-β-D-glucose
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium |
Other name(s): |
1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(2"-O-xylosyl-6"-O-glucosylgalactoside) 6′′′-O-(4-hydroxycinnamoyl)transferase |
Systematic name: |
1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) 6′′′-O-(4-hydroxycinnamoyl)transferase |
Comments: |
Isolated from the plant Daucus carota (Afghan cultivar carrot). In addition to 1-O-(4-hydroxycinnamoyl)-β-D-glucose, the enzyme can use the 1-O-sinapoyl- and 1-O-feruloyl- derivatives of β-D-glucose.
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Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Gläßgen, W.E. and Seitz, H.U. Acylation of anthocyanins with hydroxycinnamic acids via 1-O-acylglucosides by protein preparations from cell cultures of Daucus carota L. Planta 186 (1992) 582–585. [PMID: 24186789] |
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[EC 2.3.1.213 created 2013] |
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