EC |
3.2.1.64 | Relevance: 100% |
Accepted name: |
2,6-β-fructan 6-levanbiohydrolase |
Reaction: |
Hydrolysis of (2→6)-β-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(β-D-fructofuranosyl)-D-fructose, from the end of the chain |
Other name(s): |
β-2,6-fructan-6-levanbiohydrolase; 2,6-β-D-fructan 6-levanbiohydrolase; levanbiose-producing levanase; 2,6-β-D-fructan 6-β-D-fructofuranosylfructohydrolase |
Systematic name: |
(2→6)-β-D-fructofuranan 6-(β-D-fructosyl)-D-fructose-hydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-46-3 |
References: |
1. |
Avigad, G. and Zelikson, R. Cleavage of fructans to levanbiose by a specific hydrolase. Bull. Res. Counc. Isr. 11 (1963) 253–257. |
2. |
Saito, K., Kondo, K., Kojima, I., Yokota, A. and Tomita, F. Purification and characterization of 2,6-β-D-fructan 6-levanbiohydrolase from Streptomyces exfoliatus F3-2. Appl. Environ. Microbiol. 66 (2000) 252–256. [DOI] [PMID: 10618232] |
3. |
Saito, K., Oda, Y., Tomita, F. and Yokota, A. Molecular cloning of the gene for 2,6-β-D-fructan 6-levanbiohydrolase from Streptomyces exfoliatus F3-2. FEMS Microbiol. Lett. 218 (2003) 265–270. [DOI] [PMID: 12586402] |
4. |
Song, E.K., Kim, H., Sung, H.K. and Cha, J. Cloning and characterization of a levanbiohydrolase from Microbacterium laevaniformans ATCC 15953. Gene 291 (2002) 45–55. [DOI] [PMID: 12095678] |
5. |
Kang, E.J., Lee, S.O., Lee, J.D., Lee, T.H. and Lee, T.H. Purification and characterization of a levanbiose-producing levanase from Pseudomonas sp. No. 43. Biotechnol. Appl. Biochem. 29 (1999) 263–268. [PMID: 10334957] |
|
[EC 3.2.1.64 created 1972, modified 2004] |
|
|
|
|
EC |
2.4.1.206 | Relevance: 99.5% |
Accepted name: |
lactosylceramide 1,3-N-acetyl-β-D-glucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
|
For diagram of lactotetraosylceramide biosynthesis, click here |
Glossary: |
lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
lactotriosylceramide = N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
Other name(s): |
LA2 synthase; β1→3-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-lactosylceramide β-acetylglucosaminyltransferase; lactosylceramide β-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:D-galactosyl-1,4-β-D-glucosylceramide β-1,3-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 3-β-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-N-acetylglucosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-N-acetylglucosaminyltransferase (configuration-inverting) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83682-80-8 |
References: |
1. |
Gottfries, J., Percy, A.K., Maansson, J.-E., Fredman, P., Wilkstrand, C.J., Friedman, H.S., Bigner, D.D. and Svennerholm, L. Glycolipids and glycosyltransferases in permanent cell lines established from human medulloblastomas. Biochim. Biophys. Acta 1081 (1991) 253–261. [DOI] [PMID: 1825612] |
2. |
Holmes, E.H., Hakomori, S. and Ostrander, G.K. Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β1→3N-acetylglucosaminyltransferase. J. Biol. Chem. 262 (1987) 15649–15658. [PMID: 2960671] |
3. |
Percy, A.K., Gottfries, J., Vilbergsson, G., Maansson, J.E. and Svennerholm, J. Glycosphingolipid glycosyltransferases in human fetal brain. J. Neurochem. 56 (1991) 1461–1465. [DOI] [PMID: 1901591] |
|
[EC 2.4.1.206 created 1992] |
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|
|
|
EC |
3.2.1.78 | Relevance: 98.7% |
Accepted name: |
mannan endo-1,4-β-mannosidase |
Reaction: |
Random hydrolysis of (1→4)-β-D-mannosidic linkages in mannans, galactomannans and glucomannans |
Other name(s): |
endo-1,4-β-mannanase; endo-β-1,4-mannase; β-mannanase B; β-1,4-mannan 4-mannanohydrolase; endo-β-mannanase; β-D-mannanase; 1,4-β-D-mannan mannanohydrolase |
Systematic name: |
4-β-D-mannan mannanohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-54-3 |
References: |
1. |
Eriksson, A.F.V. Purification and characterisation of a fungal β-mannanase. Acta Chem. Scand. 22 (1968) 1924–1934. |
2. |
Reese, E.T. β-Mannanases of fungi. Can. J. Microbiol. 11 (1965) 167–183. [PMID: 14323029] |
|
[EC 3.2.1.78 created 1972] |
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|
|
|
EC |
3.2.1.25 | Relevance: 98.4% |
Accepted name: |
β-mannosidase |
Reaction: |
Hydrolysis of terminal, non-reducing β-D-mannose residues in β-D-mannosides |
Other name(s): |
mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase |
Systematic name: |
β-D-mannoside mannohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-43-8 |
References: |
1. |
Adams, M., Richtmyer, N.K. and Hudson, C.S. Some enzymes present in highly purified invertase preparations; a contribution to the study of fructofuranosidases, galactosidases, glucosidases and mannosidases. J. Am. Chem. Soc. 65 (1943) 1369–1380. |
2. |
Bartholomew, B.A. and Perry, A.L. The properties of synovial fluid β-mannosidase activity. Biochim. Biophys. Acta 315 (1973) 123–127. [DOI] [PMID: 4743897] |
3. |
Deuel, H., Lewuenberger, R. and Huber, G. Über den enzymatischen Abbau von Carubin, dem Galaktomannan aus Ceratonia siliqua L. Helv. Chim. Acta 33 (1950) 942–946. |
4. |
Hylin, J.W. and Sawai, K. The enzymatic hydrolysis of Leucaena glauca galactomannan. Isolation of crystalline galactomannan depolymerase. J. Biol. Chem. 239 (1964) 990–992. [PMID: 14165949] |
|
[EC 3.2.1.25 created 1961] |
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|
|
EC |
3.2.1.72 | Relevance: 98.4% |
Accepted name: |
xylan 1,3-β-xylosidase |
Reaction: |
Hydrolysis of successive xylose residues from the non-reducing termini of (1→3)-β-D-xylans |
Other name(s): |
1,3-β-D-xylosidase; exo-1,3-β-xylosidase; β-1,3′-xylanase; exo-β-1,3′-xylanase; 1,3-β-D-xylan xylohydrolase |
Systematic name: |
3-β-D-xylan xylohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-50-9 |
References: |
1. |
Fukui, S., Suzuki, T., Kitahara, K. and Miwa, T. β-1,3′-Xylanase. J. Gen. Appl. Microbiol. 6 (1960) 270–282. |
|
[EC 3.2.1.72 created 1972] |
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|
|
EC |
2.7.11.15 | Relevance: 98.3% |
Accepted name: |
β-adrenergic-receptor kinase |
Reaction: |
ATP + [β-adrenergic receptor] = ADP + phospho-[β-adrenergic receptor] |
Other name(s): |
ATP:β-adrenergic-receptor phosphotransferase; [β-adrenergic-receptor] kinase; β-adrenergic receptor-specific kinase; β-AR kinase; β-ARK; β-ARK 1; β-ARK 2; β-receptor kinase; GRK2; GRK3; β-adrenergic-receptor kinase (phosphorylating); β2ARK; βARK1; β-adrenoceptor kinase; β-adrenoceptor kinase 1; β-adrenoceptor kinase 2; ADRBK1; BARK1; adrenergic receptor kinase; STK15 |
Systematic name: |
ATP:[β-adrenergic receptor] phosphotransferase |
Comments: |
Requires G-protein for activation and therefore belongs to the family of G-protein-dependent receptor kinases (GRKs). Acts on the agonist-occupied form of the receptor; also phosphorylates rhodopsin, but more slowly. Does not act on casein or histones. The enzyme is inhibited by Zn2+ and digitonin but is unaffected by cyclic-AMP (cf. EC 2.7.11.14, rhodopsin kinase and EC 2.7.11.16, G-protein-coupled receptor kinase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102925-39-3 |
References: |
1. |
Benovic, J.L., Mayor, F., Jr., Staniszewski, C., Lefkowitz, R.J. and Caron, M.G. Purification and characterization of the β-adrenergic receptor kinase. J. Biol. Chem. 262 (1987) 9026–9032. [PMID: 3036840] |
2. |
Kim, C.M., Dion, S.B., Onorato, J.J. and Benovic, J.L. Expression and characterization of two β-adrenergic receptor kinase isoforms using the baculovirus expression system. Receptor 3 (1993) 39–55. [PMID: 8394172] |
3. |
Laugwitz, K.L., Kronsbein, K., Schmitt, M., Hoffmann, K., Seyfarth, M., Schomig, A. and Ungerer, M. Characterization and inhibition of β-adrenergic receptor kinase in intact myocytes. Cardiovasc Res 35 (1997) 324–333. [PMID: 9349395] |
4. |
Ferguson, S.S., Menard, L., Barak, L.S., Koch, W.J., Colapietro, A.M. and Caron, M.G. Role of phosphorylation in agonist-promoted β2-adrenergic receptor sequestration. Rescue of a sequestration-defective mutant receptor by betaARK1. J. Biol. Chem. 270 (1995) 24782–24789. [DOI] [PMID: 7559596] |
5. |
Willets, J.M., Challiss, R.A. and Nahorski, S.R. Non-visual GRKs: are we seeing the whole picture? Trends Pharmacol. Sci. 24 (2003) 626–633. [DOI] [PMID: 14654303] |
|
[EC 2.7.11.15 created 1989 as EC 2.7.1.126, transferred 2005 to EC 2.7.11.15] |
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EC |
2.4.1.179 | Relevance: 98.1% |
Accepted name: |
lactosylceramide β-1,3-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + β-D-galactosyl-(1→4)-β-D-glucosyl-R = UDP + β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-R |
|
For diagram of glycolipid biosynthesis, click here |
Glossary: |
lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
Other name(s): |
uridine diphosphogalactose-lactosylceramide β1→3-galactosyltransferase; UDP-galactose:D-galactosyl-1,4-β-D-glucosyl-R β-1,3-galactosyltransferase; UDP-galactose:D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase; UDP-α-D-galactose:D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase |
Systematic name: |
UDP-α-D-galactose:β-D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase |
Comments: |
R may be an oligosaccharide or a glycolipid; lactose can also act as acceptor, but more slowly. Involved in the elongation of oligosaccharide chains, especially in glycolipids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 106769-64-6 |
References: |
1. |
Bailly, P., Piller, F. and Cartron, J.-P. Characterization and specific assay for a galactoside β-3-galactosyltransferase of human kidney. Eur. J. Biochem. 173 (1988) 417–422. [DOI] [PMID: 3129295] |
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[EC 2.4.1.179 created 1989] |
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|
EC |
3.4.19.5 | Relevance: 97.9% |
Accepted name: |
β-aspartyl-peptidase |
Reaction: |
Cleavage of a β-linked Asp residue from the N-terminus of a polypeptide |
Other name(s): |
β-aspartyl dipeptidase; β-aspartyl peptidase; β-aspartyldipeptidase |
Comments: |
Other isopeptide bonds, e.g. γ-glutamyl and β-alanyl, are not hydrolysed. A mammalian, cytosolic enzyme. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-74-7 |
References: |
1. |
Haley, E.E. β-Aspartyl peptidase from rat liver. Methods Enzymol. 19 (1970) 737–741. |
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[EC 3.4.19.5 created 1972 as EC 3.4.13.10, transferred 1992 to EC 3.4.19.5, modified 1997] |
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|
|
|
EC |
3.2.1.73 | Relevance: 97.8% |
Accepted name: |
licheninase |
Reaction: |
Hydrolysis of (1→4)-β-D-glucosidic linkages in β-D-glucans containing (1→3)- and (1→4)-bonds |
Other name(s): |
lichenase; β-(1→4)-D-glucan 4-glucanohydrolase; 1,3;1,4-β-glucan endohydrolase; 1,3;1,4-β-glucan 4-glucanohydrolase; 1,3-1,4-β-D-glucan 4-glucanohydrolase |
Systematic name: |
(1→3)-(1→4)-β-D-glucan 4-glucanohydrolase |
Comments: |
Acts on lichenin and cereal β-D-glucans, but not on β-D-glucans containing only 1,3- or 1,4-bonds. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-51-0 |
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 3.2.1.73 created 1972] |
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|
EC |
3.2.1.32 | Relevance: 97.7% |
Accepted name: |
endo-1,3-β-xylanase |
Reaction: |
Random endohydrolysis of (1→3)-β-D-glycosidic linkages in (1→3)-β-D-xylans |
Other name(s): |
xylanase (ambiguous); endo-1,3-β-xylosidase (misleading); 1,3-β-xylanase; 1,3-xylanase; β-1,3-xylanase; endo-β-1,3-xylanase; 1,3-β-D-xylan xylanohydrolase; xylan endo-1,3-β-xylosidase |
Systematic name: |
3-β-D-xylan xylanohydrolase |
Comments: |
This enzyme is found mostly in marine bacteria, which break down the β(1,3)-xylan found in the cell wall of some green and red algae. The enzyme produces mainly xylobiose, xylotriose and xylotetraose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-55-2 |
References: |
1. |
Chen, W.P., Matsuo, M. and Tsuneo, Y. Purification and some properties of β-1,3-xylanase from Aspergillus terreus A-07. Agric. Biol. Chem. 50 (1986) 1183–1194. |
2. |
Aoki, T., Araki, T. and Kitamikado, M. Purification and characterization of an endo-β-1,3-xylanase from Vibrio species. Nippon Suisan Gakkaishi 54 (1988) 277–281. |
3. |
Araki, T., Tani, S., Maeda, K., Hashikawa, S., Nakagawa, H. and Morishita, T. Purification and characterization of β-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214. Biosci. Biotechnol. Biochem. 63 (1999) 2017–2019. [PMID: 10635569] |
4. |
Araki, T., Inoue, N. and Morishita, T. Purification and characterization of β-1,3-xylanase from a marine bacterium, Alcaligenes sp. XY-234. J. Gen. Appl. Microbiol. 44 (1998) 269–274. [PMID: 12501421] |
5. |
Okazaki, F., Shiraki, K., Tamaru, Y., Araki, T. and Takagi, M. The first thermodynamic characterization of β-1,3-xylanase from a marine bacterium. Protein J. 24 (2005) 413–421. [DOI] [PMID: 16328734] |
|
[EC 3.2.1.32 created 1965, modified 2011] |
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|
|
EC |
3.2.1.153 | Relevance: 97.6% |
Accepted name: |
fructan β-(2,1)-fructosidase |
Reaction: |
Hydrolysis of terminal, non-reducing (2→1)-linked β-D-fructofuranose residues in fructans |
|
For diagram of reaction, click here |
Other name(s): |
β-(2-1)-D-fructan fructohydrolase; β-(2-1)fructan exohydrolase; inulinase; 1-FEH II; 1-fructan exohydrolase; 1-FEH w1; 1-FEH w2; β-(2-1)-linkage-specific fructan-β-fructosidase; β-(2,1)-D-fructan fructohydrolase |
Systematic name: |
β-(2→1)-D-fructan fructohydrolase |
Comments: |
Possesses one of the activities of EC 3.2.1.80, fructan β-fructosidase. While the best substrates are the inulin-type fructans, such as 1-kestose [β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside] and 1,1-nystose [β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside], some (but not all) levan-type fructans can also be hydrolysed, but more slowly [see EC 3.2.1.154, fructan β-(2,6)-fructosidase]. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1000593-08-7 |
References: |
1. |
De Roover, J., Van Laere, A., De Winter, M., Timmermans, J.W. and Van den Ende, W. Purification and properties of a second fructan exohydrolase from the roots of Cichorium intybus. Physiol. Plant. 106 (1999) 28–34. |
2. |
Van den Ende, W., Clerens, S., Vergauwen, R., Van Riet, L., Van Laere, A., Yoshida, M. and Kawakami, A. Fructan 1-exohydrolases. β-(2,1)-Trimmers during graminan biosynthesis in stems of wheat? Purification, characterization, mass mapping, and cloning of two fructan 1-exohydrolase isoforms. Plant Physiol. 131 (2003) 621–631. [DOI] [PMID: 12586886] |
|
[EC 3.2.1.153 created 2005] |
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|
EC |
3.2.1.197 | Relevance: 97.1% |
Accepted name: |
β-1,2-mannosidase |
Reaction: |
β-D-mannopyranosyl-(1→2)-β-D-mannopyranosyl-(1→2)-D-mannopyranose + H2O = β-D-mannopyranosyl-(1→2)-D-mannopyranose + α-D-mannopyranose |
Systematic name: |
β-1,2-D-mannoside mannohydrolase |
Comments: |
The enzyme, characterized from multiple bacterial species, catalyses the hydrolysis of terminal, non-reducing D-mannose residues from β-1,2-mannotriose and β-1,2-mannobiose. The mechanism involves anomeric inversion, resulting in the release of α-D-mannopyranose. Activity with β-1,2-mannotriose or higher oligosaccharides is higher than that with β-1,2-mannobiose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Cuskin, F., Basle, A., Ladeveze, S., Day, A.M., Gilbert, H.J., Davies, G.J., Potocki-Veronese, G. and Lowe, E.C. The GH130 family of mannoside phosphorylases contains glycoside hydrolases that target β-1,2-mannosidic linkages in Candida mannan. J. Biol. Chem. 290 (2015) 25023–25033. [DOI] [PMID: 26286752] |
2. |
Nihira, T., Chiku, K., Suzuki, E., Nishimoto, M., Fushinobu, S., Kitaoka, M., Ohtsubo, K. and Nakai, H. An inverting β-1,2-mannosidase belonging to glycoside hydrolase family 130 from Dyadobacter fermentans. FEBS Lett. 589 (2015) 3604–3610. [DOI] [PMID: 26476324] |
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[EC 3.2.1.197 created 2016] |
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|
EC |
3.2.1.100 | Relevance: 97% |
Accepted name: |
mannan 1,4-mannobiosidase |
Reaction: |
Hydrolysis of (1→4)-β-D-mannosidic linkages in (1→4)-β-D-mannans, to remove successive mannobiose residues from the non-reducing chain ends |
Other name(s): |
1,4-β-D-mannan mannobiohydrolase; exo-β-mannanase; exo-1,4-β-mannobiohydrolase |
Systematic name: |
4-β-D-mannan mannobiohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81811-49-6 |
References: |
1. |
Araki, T. and Kitamikado, M. Purification and characterization of a novel exo-β-mannanase from Aeromonas sp. F-25. J. Biochem. (Tokyo) 91 (1982) 1181–1186. [PMID: 7096283] |
|
[EC 3.2.1.100 created 1983] |
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|
|
EC |
2.7.8.17 | Relevance: 96.6% |
Accepted name: |
UDP-N-acetylglucosamine—lysosomal-enzyme N-acetylglucosaminephosphotransferase |
Reaction: |
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose |
Other name(s): |
N-acetylglucosaminylphosphotransferase; UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase; UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase; uridine diphosphoacetylglucosamine-lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase; uridine diphosphoacetylglucosamine-glycoprotein acetylglucosamine-1-phosphotransferase; lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase; N-acetylglucosaminyl phosphotransferase; UDP-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase; UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase; UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase; UDP-N-acetylglucosamine:glycoprotein N-acetylglucosaminyl-1-phosphotransferase |
Systematic name: |
UDP-N-acetyl-D-glucosamine:lysosomal-enzyme N-acetylglucosaminephosphotransferase |
Comments: |
Some other glycoproteins with high-mannose can act as acceptors, but much more slowly than lysosomal enzymes. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 84012-69-1 |
References: |
1. |
Reitman, M.L. and Kornfeld, S. UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase. Proposed enzyme for the phosphorylation of the high mannose oligosaccharide units of lysosomal enzymes. J. Biol. Chem. 256 (1981) 4275–4281. [PMID: 6452459] |
2. |
Reitman, M.L. and Kornfeld, S. Lysosomal enzyme targeting. N-Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes. J. Biol. Chem. 256 (1981) 11977–11980. [PMID: 6457829] |
3. |
Waheed, A., Hasilik, A. and von Figura, K. UDP-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase. Partial purification and characterization of the rat liver Golgi enzyme. J. Biol. Chem. 257 (1982) 12322–12331. [PMID: 6288715] |
4. |
Waheed, A., Pohlmann, R., Hasilik, A. and von Figura, K. Subcellular location of two enzymes involved in the synthesis of phosphorylated recognition markers in lysosomal enzymes. J. Biol. Chem. 256 (1981) 4150–4152. [PMID: 6260788] |
|
[EC 2.7.8.17 created 1984] |
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|
|
|
EC |
3.2.1.58 | Relevance: 96.6% |
Accepted name: |
glucan 1,3-β-glucosidase |
Reaction: |
Successive hydrolysis of β-D-glucose units from the non-reducing ends of (1→3)-β-D-glucans, releasing α-glucose |
Other name(s): |
exo-1,3-β-glucosidase; β-1,3-glucan exo-hydrolase; exo (1→3)-glucanohydrolase; 1,3-β-glucan glucohydrolase |
Systematic name: |
3-β-D-glucan glucohydrolase |
Comments: |
Acts on oligosaccharides, but very slowly on laminaribiose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9073-49-8 |
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] |
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[EC 3.2.1.58 created 1972] |
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EC
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1.13.12.12
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Transferred entry: | apo-β-carotenoid-14′,13′-dioxygenase. The enzyme was misclassified and has been transferred to EC 1.13.11.67, 8-apo-β-carotenoid 14′,13′-cleaving dioxygenase
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[EC 1.13.12.12 created 2000, modified 2001, deleted 2012] |
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EC |
3.2.1.185 | Relevance: 96.4% |
Accepted name: |
non-reducing end β-L-arabinofuranosidase |
Reaction: |
β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranose + H2O = 2 β-L-arabinofuranose |
Other name(s): |
HypBA1 |
Systematic name: |
β-L-arabinofuranoside non-reducing end β-L-arabinofuranosidase |
Comments: |
The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, removes the β-L-arabinofuranose residue from the non-reducing end of multiple substrates, including β-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara2-Hyp, Ara3-Hyp, and β-L-arabinofuranosyl-(1→2)-1-O-methyl-β-L-arabinofuranose.In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. cf. EC 3.2.1.55, non-reducing end α-L-arabinofuranosidase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Fujita, K., Takashi, Y., Obuchi, E., Kitahara, K. and Suganuma, T. Characterization of a novel β-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 protein family member. J. Biol. Chem. 289 (2014) 5240–5249. [DOI] [PMID: 24385433] |
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[EC 3.2.1.185 created 2013] |
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EC |
2.4.1.275 | Relevance: 95.9% |
Accepted name: |
neolactotriaosylceramide β-1,4-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
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For diagram of neolactotetraosylceramide biosynthesis, click here |
Glossary: |
N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = neolactotriaosylceramide |
Other name(s): |
β4Gal-T4; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase; lactotriaosylceramide β-1,4-galactosyltransferase (incorrect) |
Systematic name: |
UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-D-galactosyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Schwientek, T., Almeida, R., Levery, S.B., Holmes, E.H., Bennett, E. and Clausen, H. Cloning of a novel member of the UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis. J. Biol. Chem. 273 (1998) 29331–29340. [DOI] [PMID: 9792633] |
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[EC 2.4.1.275 created 2011, modified 2013] |
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EC |
3.2.1.43 | Relevance: 95.8% |
Accepted name: |
β-L-rhamnosidase |
Reaction: |
Hydrolysis of terminal, non-reducing β-L-rhamnose residues in β-L-rhamnosides |
Systematic name: |
β-L-rhamnoside rhamnohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-37-2 |
References: |
1. |
Barker, S.A., Somers, P.J. and Stacey, M. Arrangement of the L-rhamnose units in Diplococcus pneumoniae type II polysaccharide. Carbohydr. Res. 1 (1965) 106–115. |
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[EC 3.2.1.43 created 1972] |
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EC |
3.2.1.154 | Relevance: 95.7% |
Accepted name: |
fructan β-(2,6)-fructosidase |
Reaction: |
Hydrolysis of terminal, non-reducing (2→6)-linked β-D-fructofuranose residues in fructans |
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For diagram of reaction, click here |
Other name(s): |
β-(2-6)-fructan exohydrolase; levanase; 6-FEH; β-(2,6)-D-fructan fructohydrolase |
Systematic name: |
(2→6)-β-D-fructan fructohydrolase |
Comments: |
Possesses one of the activities of EC 3.2.1.80, fructan β-fructosidase. While the best substrates are the levan-type fructans such as 6-kestotriose [β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl α-D-glucopyranoside] and 6,6-kestotetraose [β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl α-D-glucopyranoside], some (but not all) inulin-type fructans can also be hydrolysed, but more slowly [cf. EC 3.2.1.153, fructan β-(2,1)-fructosidase]. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 1000597-62-5 |
References: |
1. |
Marx, S.P., Nösberger, J. and Frehner, M. Hydrolysis of fructan in grasses: A β-(2-6)-linkage specific fructan-β-fructosidase from stubble of Lolium perenne. New Phytol. 135 (1997) 279–290. |
2. |
Van den Ende, W., De Coninck, B., Clerens, S., Vergauwen, R. and Van Laere, A. Unexpected presence of fructan 6-exohydrolases (6-FEHs) in non-fructan plants: characterization, cloning, mass mapping and functional analysis of a novel 'cell-wall invertase-like' specific 6-FEH from sugar beet (Beta vulgaris L.). Plant J. 36 (2003) 697–710. [DOI] [PMID: 14617070] |
3. |
Henson, C.A. and Livingston, D.P. , III. Purification and characterization of an oat fructan exohydrolase that preferentially hydrolyzes β-2,6-fructans. Plant Physiol. 110 (1996) 639–644. [PMID: 8742337] |
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[EC 3.2.1.154 created 2005] |
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EC |
3.2.1.181 | Relevance: 95.6% |
Accepted name: |
galactan endo-β-1,3-galactanase |
Reaction: |
The enzyme specifically hydrolyses β-1,3-galactan and β-1,3-galactooligosaccharides |
Other name(s): |
endo-β-1,3-galactanase |
Systematic name: |
arabinogalactan 3-β-D-galactanohydrolase |
Comments: |
The enzyme from the fungus Flammulina velutipes (winter mushroom) hydrolyses the β(1→3) bonds found in type II plant arabinogalactans, which occur in cell walls of dicots and cereals. The enzyme is an endohydrolase, and requires at least 3 contiguous β-1,3-residues. cf. EC 3.2.1.89, arabinogalactan endo-β-1,4-galactanase and EC 3.2.1.145, galactan 1,3-β-galactosidase.
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Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kotake, T., Hirata, N., Degi, Y., Ishiguro, M., Kitazawa, K., Takata, R., Ichinose, H., Kaneko, S., Igarashi, K., Samejima, M. and Tsumuraya, Y. Endo-β-1,3-galactanase from winter mushroom Flammulina velutipes. J. Biol. Chem. 286 (2011) 27848–27854. [DOI] [PMID: 21653698] |
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[EC 3.2.1.181 created 2012] |
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EC |
2.4.1.249 | Relevance: 95.5% |
Accepted name: |
delphinidin 3′,5′-O-glucosyltransferase |
Reaction: |
2 UDP-glucose + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside = 2 UDP + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′,5′-di-O-β-D-glucoside (overall reaction) (1a) UDP-glucose + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside = UDP + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′-O-β-D-glucoside (1b) UDP-glucose + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′-O-β-D-glucoside = UDP + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′,5′-di-O-β-D-glucoside |
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For diagram of anthocyanidin acylglucoside biosynthesis, click here |
Glossary: |
delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′,5′-di-O-β-D-glucoside = ternatin C5 |
Other name(s): |
UDP-glucose:anthocyanin 3′,5′-O-glucosyltransferase; UA3′5’GZ |
Systematic name: |
UDP-glucose:delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside 3′-O-glucosyltransferase |
Comments: |
Ternatins are a group of polyacetylated delphinidin glucosides that confer
blue color to the petals of Clitoria ternatea (butterfly pea).
This enzyme catalyses two reactions in the biosynthesis of ternatin C5: the conversion of delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside to delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′-O-β-D-glucoside, followed by the conversion of the later to ternatin C5, by transferring two glucosyl groups in a stepwise manner [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kogawa, K., Kato, N., Kazuma, K., Noda, N. and Suzuki, M. Purification and characterization of UDP-glucose: anthocyanin 3′,5′-O-glucosyltransferase from Clitoria ternatea. Planta 226 (2007) 1501–1509. [DOI] [PMID: 17668234] |
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[EC 2.4.1.249 created 2009] |
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EC |
2.4.1.38 | Relevance: 95.5% |
Accepted name: |
β-N-acetylglucosaminylglycopeptide β-1,4-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + N-acetyl-β-D-glucosaminylglycopeptide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminylglycopeptide |
Other name(s): |
UDP-galactose—glycoprotein galactosyltransferase; glycoprotein 4-β-galactosyl-transferase; β-N-acetyl-β1-4-galactosyltransferase; thyroid glycoprotein β-galactosyltransferase; glycoprotein β-galactosyltransferase; thyroid galactosyltransferase; uridine diphosphogalactose-glycoprotein galactosyltransferase; β-N-acetylglucosaminyl-glycopeptide β-1,4-galactosyltransferase; GalT; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide β-1,4-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase |
Systematic name: |
UDP-α-D-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase |
Comments: |
Terminal N-acetyl-β-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. High activity is shown towards such residues in branched-chain polysaccharides when these are linked by β-1,6-links to galactose residues; lower activity towards residues linked to galactose by β-1,3-links. A component of EC 2.4.1.22 (lactose synthase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37237-43-7 |
References: |
1. |
Beyer, T.A., Sadler, J.E., Rearick, J.I., Paulson, J.C. and Hill, R.L. Glucosyltransferases and their uses in assessing oligosaccharide structure and structure-function relationship. Adv. Enzymol. 52 (1981) 23–175. [PMID: 6784450] |
2. |
Blanken, W.M., Hooghwinkel, G.J.M. and van den Eijnden, D.H. Biosynthesis of blood-group I and i substances. Specificity of bovine colostrum β-N-acetyl-D-glucosaminide β1→4 galactosyltransferase. Eur. J. Biochem. 127 (1982) 547–552. [DOI] [PMID: 6816588] |
3. |
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] |
4. |
Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid galactosyltransferase. J. Biol. Chem. 243 (1968) 6529–6537. [PMID: 5726898] |
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[EC 2.4.1.38 created 1972, modified 1976, modified 1980, modified 1986] |
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EC |
3.2.1.4 | Relevance: 94.7% |
Accepted name: |
cellulase |
Reaction: |
Endohydrolysis of (1→4)-β-D-glucosidic linkages in cellulose, lichenin and cereal β-D-glucans |
Other name(s): |
endo-1,4-β-D-glucanase; β-1,4-glucanase; β-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS; 1,4-(1,3;1,4)-β-D-glucan 4-glucanohydrolase |
Systematic name: |
4-β-D-glucan 4-glucanohydrolase |
Comments: |
Will also hydrolyse 1,4-linkages in β-D-glucans also containing 1,3-linkages. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-54-8 |
References: |
1. |
Datta, P.K., Hanson, K.R. and Whitaker, D.R. Improved procedures for preparation and characterization of Myrothecum cellulase. III. Molecular weight, amino acid composition, terminal residues, and other properties. Can. J. Biochem. Physiol. 41 (1963) 697–705. [PMID: 14025219] |
2. |
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. |
3. |
Myers, F.L. and Northcote, D.H. Partial purification and some properties of a cellulase from Helix pomatia. Biochem. J. 71 (1959) 749–756. [PMID: 13651124] |
4. |
Nishizawa, K. and Hashimoto, Y. Cellulose splitting enzymes. VI. Difference in the specificities of cellulase and β-glucosidase from Irpex lacteus. Arch. Biochem. Biophys. 81 (1959) 211–222. [PMID: 13637982] |
5. |
Whitaker, D.R., Hanson, K.R. and Datta, P.K. Improved procedures for preparation and characterization of myrothecium cellulase. 2. Purification procedures. Can. J. Biochem. Physiol. 41 (1963) 671–696. [PMID: 14000266] |
6. |
Hatfield, R. and Nevins, D.J. Purification and properties of an endoglucanase isolated from the cell walls of Zea mays seedlings. Carbohydr. Res. 148 (1986) 265–278. |
7. |
Hatfield, R. and Nevins, D.J. Hydrolytic activity and substrate specificity of an endoglucanase from Zea mays seedling cell walls. Plant Physiol. 83 (1987) 203–207. [PMID: 16665203] |
8. |
Inohue, M., Hayashgi, K. and Nevins, D.J. Polypeptide characteristics and immunological properties of exo- and endoglucanases purified from maize coleoptile cell walls. J. Plant Physiol. 154 (1999) 334–340. |
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[EC 3.2.1.4 created 1961, modified 2001] |
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EC |
3.2.1.145 | Relevance: 94.6% |
Accepted name: |
galactan 1,3-β-galactosidase |
Reaction: |
Hydrolysis of terminal, non-reducing β-D-galactose residues in (1→3)-β-D-galactopyranans |
Other name(s): |
galactan (1→3)-β-D-galactosidase |
Systematic name: |
galactan 3-β-D-galactosidase |
Comments: |
This enzyme removes not only free galactose, but also 6-glycosylated residues, e.g., (1→6)-β-D-galactobiose, and galactose bearing oligosaccharide chains on O-6. Hence, it releases branches from [arabino-galacto-(1→6)]-(1→3)-β-D-galactans. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 161515-48-6 |
References: |
1. |
Tsumuraya, Y., Mochizuki, N. , Hashimoto Y. and Kovac, P. Purification of exo-(1→3)-D-galactanase of Irpex lacteus (Polyporus tulipiferae) and its action on arabinogalactan-proteins. J. Biol. Chem. 265 (1990) 7207–7215. [PMID: 2158993] |
2. |
Pellerin, P. and Brillouet, J.M. Purification and properties of an exo-(1→3)-β-D-galactanase from Aspergillus niger. Carbohydr. Res. 264 (1994) 281–291. [DOI] [PMID: 7805066] |
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[EC 3.2.1.145 created 2001] |
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EC |
3.2.1.53 | Relevance: 94.3% |
Accepted name: |
β-N-acetylgalactosaminidase |
Reaction: |
Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-β-D-galactosaminides |
Other name(s): |
N-acetyl-β-galactosaminidase; N-acetyl-β-D-galactosaminidase; β-acetylgalactosaminidase; β-D-N-acetylgalactosaminidase; N-acetylgalactosaminidase |
Systematic name: |
β-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-43-7 |
References: |
1. |
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] |
2. |
Hoogwinkel, G.J.M., Veltkamp, W.A., Overdijk, B. and Lisman, J.W. Electrophoretic separation of β-N-acetylhexosaminidases of human and bovine brain and liver and of Tay-Sachs brain tissue. Hoppe-Seylers Z. Physiol. Chem. 353 (1972) 839–841. [PMID: 5069351] |
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[EC 3.2.1.53 created 1972] |
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EC |
3.2.1.146 | Relevance: 93.9% |
Accepted name: |
β-galactofuranosidase |
Reaction: |
Hydrolysis of terminal non-reducing β-D-galactofuranosides, releasing galactose |
Other name(s): |
exo-β-galactofuranosidase; exo-β-D-galactofuranosidase; β-D-galactofuranosidase |
Systematic name: |
β-D-galactofuranoside hydrolase |
Comments: |
The enzyme from Helminthosporium sacchari detoxifies helminthosporoside, a bis(digalactosyl)terpene produced by this fungus, by releasing its four molecules of bound galactose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52357-57-0 |
References: |
1. |
Rietschel-Berst, M., Jentoft, N.H., Rick, P.D., Pletcher, C., Fang, F. and Gander, J.E. Extracellular exo-β-galactofuranosidase from Penicillium charlesii: isolation, purification, and properties. J. Biol. Chem. 252 (1977) 3219–3226. [PMID: 863879] |
2. |
Daley, L.S. and Strobel, G.A. β-Galactofuranosidase activity in Helminthosporium sacchari and its relationship to the production of helminthosporoside. Plant Sci. Lett. 30 (1983) 145–154. |
3. |
Cousin, M.A., Notermans, S., Hoogerhout, P. and Van Boom, J.H. Detection of β-galactofuranosidase production by Penicillium and Aspergillus species using 4-nitrophenyl β-D-galactofuranoside. J. Appl. Bacteriol. 66 (1989) 311–317. [PMID: 2502527] |
4. |
Miletti, L.C., Marino, C., Marino, K., de Lederkremer, R.M., Colli, W. and Alves, M.J.M. Immobilized 4-aminophenyl-1-thio-β-D-galactofuranoside as a matrix for affinity purification of an exo-β-D-galactofuranosidase. Carbohydr. Res. 320 (1999) 176–182. [DOI] [PMID: 10573856] |
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[EC 3.2.1.146 created 2001] |
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EC
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2.4.99.2
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Transferred entry: | β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase. Now EC 2.4.3.2, β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase
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[EC 2.4.99.2 created 1976, modified 1986, deleted 2022] |
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EC |
2.4.3.2 | Relevance: 93.3% |
Accepted name: |
β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R = CMP + an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R |
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For diagram of ganglioside biosynthesis, click here |
Glossary: |
a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GM1a
an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GD1a |
Other name(s): |
CMP-N-acetylneuraminate:D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-(1↔1)-ceramide N-acetylneuraminyltransferase (ambiguous); monosialoganglioside sialyltransferase; CMP-N-acetylneuraminate:a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide N-acetyl-β-neuraminyltransferase |
Systematic name: |
CMP-N-acetyl-β-neuraminate:a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R α-(2→3)-N-acetylneuraminyltransferase (configuration-inverting) |
Comments: |
The enzyme recognizes the sequence β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl (known as type 1 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids [1]. When acting on gangloside GM1a, it forms gangloside GD1a [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 60202-12-2 |
References: |
1. |
Rearick, J.I., Sadler, J.E., Paulson, J.C. and Hill, R.L. Enzymatic characterization of β D-galactoside α2→3 sialyltransferase from porcine submaxillary gland. J. Biol. Chem. 254 (1979) 4444–4451. [PMID: 438198] |
2. |
Yip, M.C.M. The enzymic synthesis of disialoganglioside: rat brain cytidine-5′-monophospho-N-acetylneuraminic acid: monosialoganglioside (GM1) sialyltransferase. Biochim. Biophys. Acta 306 (1973) 298–306. [DOI] [PMID: 4351506] |
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[EC 2.4.3.2 created 1976 as EC 2.4.99.2, modified 1986, modified 2017, transferred 2022 to EC 2.4.3.2] |
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EC |
3.2.1.92 | Relevance: 93.2% |
Accepted name: |
peptidoglycan β-N-acetylmuramidase |
Reaction: |
Hydrolysis of terminal, non-reducing N-acetylmuramic residues |
Other name(s): |
exo-β-N-acetylmuramidase; exo-β-acetylmuramidase; β-2-acetamido-3-O-(D-1-carboxyethyl)-2-deoxy-D-glucoside acetamidodeoxyglucohydrolase |
Systematic name: |
peptidoglycan β-N-acetylmuramoylexohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52219-03-1 |
References: |
1. |
Del Rio, L.A. and Berkeley, R.C.W. Exo-β-N-acetylmuramidase - a novel hexosaminidase. Production by Bacillus subtilis B, purification and characterization. Eur. J. Biochem. 65 (1976) 3–12. [DOI] [PMID: 6281] |
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[EC 3.2.1.92 created 1976] |
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EC |
3.2.1.26 | Relevance: 93.1% |
Accepted name: |
β-fructofuranosidase |
Reaction: |
Hydrolysis of terminal non-reducing β-D-fructofuranoside residues in β-D-fructofuranosides |
Other name(s): |
invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase |
Systematic name: |
β-D-fructofuranoside fructohydrolase |
Comments: |
Substrates include sucrose; also catalyses fructotransferase reactions. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-57-4 |
References: |
1. |
Myrbäck, K. Invertases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 379–396. |
2. |
Neumann, N.P. and Lampen, J.O. Purification and properties of yeast invertase. Biochemistry 6 (1967) 468–475. [PMID: 4963242] |
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[EC 3.2.1.26 created 1961] |
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EC |
3.2.1.214 | Relevance: 92.9% |
Accepted name: |
exo β-1,2-glucooligosaccharide sophorohydrolase (non-reducing end) |
Reaction: |
[(1→2)-β-D-glucosyl]n + H2O = sophorose + [(1→2)-β-D-glucosyl]n-2 |
Glossary: |
sophorose = β-D-glucopyranosyl-(1→2)-D-glucopyranose |
Systematic name: |
exo (1→2)-β-D-glucooligosaccharide sophorohydrolase (non-reducing end) |
Comments: |
The enzyme, characterized from the bacterium Parabacteroides distasonis, specifically hydrolyses (1→2)-β-D-glucooligosaccharides to sophorose. The best substrates are the tetra- and pentasaccharides. The enzyme is not able to cleave the trisaccharide, and activity with longer linear (1→2)-β-D-glucans is quite low. This enzyme acts in exo mode and is not able to hydrolyse cyclic (1→2)-β-D-glucans. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Shimizu, H., Nakajima, M., Miyanaga, A., Takahashi, Y., Tanaka, N., Kobayashi, K., Sugimoto, N., Nakai, H. and Taguchi, H. Characterization and structural analysis of a novel exo-type enzyme acting on β-1,2-glucooligosaccharides from Parabacteroides distasonis. Biochemistry 57 (2018) 3849–3860. [PMID: 29763309] |
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[EC 3.2.1.214 created 2020] |
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EC |
1.13.11.67 | Relevance: 92.9% |
Accepted name: |
8′-apo-β-carotenoid 14′,13′-cleaving dioxygenase |
Reaction: |
8′-apo-β-carotenol + O2 = 14′-apo-β-carotenal + an uncharacterized product |
|
For diagram of 8′-apo-β-carotenal metabolites, click here |
Other name(s): |
8′-apo-β-carotenol:O2 oxidoreductase (14′,13′-cleaving) |
Systematic name: |
8′-apo-β-carotenol:oxygen oxidoreductase (14′,13′-cleaving) |
Comments: |
A thiol-dependent enzyme isolated from rat and rabbit. Unlike EC 1.13.11.63, β-carotene-15,15′-dioxygenase, it is not active towards β-carotene. The secondary product has not been characterized, but may be (3E,5E)-7-hydroxy-6-methylhepta-3,5-dien-2-one. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 198028-39-6 |
References: |
1. |
Dmitrovskii, A.A., Gessler, N.N., Gomboeva, S.B., Ershov, Yu.V. and Bykhovsky, V.Ya. Enzymatic oxidation of β-apo-8′-carotenol to β-apo-14′-carotenal by an enzyme different from β-carotene-15,15′-dioxygenase. Biochemistry (Mosc.) 62 (1997) 787–792. [PMID: 9331970] |
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[EC 1.13.11.67 created 2000 as EC 1.13.12.12, transferred 2012 to EC 1.13.11.67] |
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EC |
2.4.1.27 | Relevance: 92.7% |
Accepted name: |
DNA β-glucosyltransferase |
Reaction: |
Transfers a β-D-glucosyl residue from UDP-α-D-glucose to an hydroxymethylcytosine residue in DNA |
Other name(s): |
T4-HMC-β-glucosyl transferase; T4-β-glucosyl transferase; T4 phage β-glucosyltransferase; UDP glucose-DNA β-glucosyltransferase; uridine diphosphoglucose-deoxyribonucleate β-glucosyltransferase; UDP-glucose:DNA β-D-glucosyltransferase |
Systematic name: |
UDP-α-D-glucose:DNA β-D-glucosyltransferase (configuration-inverting) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-14-2 |
References: |
1. |
Kornberg, S.R., Zimmerman, S.B. and Kornberg, A. Glucosylation of deoxyribonucleic acid by enzymes from bacteriophage-infected Escherichia coli. J. Biol. Chem. 236 (1961) 1487–1493. [PMID: 13753193] |
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[EC 2.4.1.27 created 1965] |
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EC |
3.2.1.71 | Relevance: 92.2% |
Accepted name: |
glucan endo-1,2-β-glucosidase |
Reaction: |
Random hydrolysis of (1→2)-glucosidic linkages in (1→2)-β-D-glucans |
Other name(s): |
endo-1,2-β-glucanase; β-D-1,2-glucanase; endo-(1→2)-β-D-glucanase; 1,2-β-D-glucan glucanohydrolase |
Systematic name: |
2-β-D-glucan glucanohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-49-6 |
References: |
1. |
Reese, E.T., Parrish, F.W. and Mandels, M. β-D-1,2-Glucanases in fungi. Can. J. Microbiol. 7 (1961) 309–317. [PMID: 13740314] |
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[EC 3.2.1.71 created 1972] |
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EC |
3.2.1.31 | Relevance: 92.2% |
Accepted name: |
β-glucuronidase |
Reaction: |
a β-D-glucuronoside + H2O = D-glucuronate + an alcohol |
Other name(s): |
β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase |
Systematic name: |
β-D-glucuronoside glucuronosohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-45-0 |
References: |
1. |
Diez, T. and Cabezas, J.A. Properties of two molecular forms of β-glucuronidase from the mollusc Littorina littorea L. Eur. J. Biochem. 93 (1978) 301–311. |
2. |
Doyle, M.L., Katzman, P.A. and Doisy, E.A. Production and properties of bacterial β-glucuronidase. J. Biol. Chem. 217 (1955) 921–930. [PMID: 13271452] |
3. |
Fishman, W.H. Beta-glucuronidase. Adv. Enzymol. Relat. Subj. Biochem. 16 (1955) 361–409. [PMID: 14376216] |
4. |
Levvy, G.A. and Marsh, C.A. β-Glucuronidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 397–407. |
5. |
Wakabayashi, M. and Fishman, W.H. The comparative ability of β-glucuronidase preparations (liver, Escherichia coli, Helix pomatia, and Patella vulgata) to hydrolyze certain steroid glucosiduronic acids. J. Biol. Chem. 236 (1961) 996–1001. [PMID: 13782588] |
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[EC 3.2.1.31 created 1961] |
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EC |
1.5.1.26 | Relevance: 92.2% |
Accepted name: |
β-alanopine dehydrogenase |
Reaction: |
β-alanopine + NAD+ + H2O = β-alanine + pyruvate + NADH + H+ |
Systematic name: |
N-(D-1-carboxyethyl)-β-alanine:NAD+ oxidoreductase (β-alanine-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 113573-64-1 |
References: |
1. |
Sato, M., Takahara, M., Kanno, N., Sato, Y. and Ellington, W.R. Isolation of a new opine, β-alanopine, from the extracts of the muscle of the marine bivalve mollusc Scapharca broughtonii. Comp. Biochem. Physiol. 88B (1987) 803–806. |
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[EC 1.5.1.26 created 1990] |
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EC
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2.4.99.1
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Transferred entry: | β-galactoside α-(2,6)-sialyltransferase. Now EC 2.4.3.1, β-galactoside α-(2,6)-sialyltransferase
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[EC 2.4.99.1 created 1972, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2017), deleted 2022] |
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EC |
2.4.3.1 | Relevance: 92.2% |
Accepted name: |
β-galactoside α-(2,6)-sialyltransferase |
Reaction: |
CMP-N-acetyl-β-neuraminate + β-D-galactosyl-R = CMP + N-acetyl-α-neuraminyl-(2→6)-β-D-galactosyl-R |
Other name(s): |
ST6Gal-I; CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase; lactosylceramide α-2,6-N-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine α-(2→6)-N-acetylneuraminyltransferase; β-galactoside α-2,6-sialyltransferase |
Systematic name: |
CMP-N-acetyl-β-neuraminate:β-D-galactoside α-(2→6)-N-acetylneuraminyltransferase (configuration-inverting) |
Comments: |
The enzyme acts on the terminal non-reducing β-D-galactosyl residue of the oligosaccharide moiety of glycoproteins and glycolipids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-81-4 |
References: |
1. |
Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid sialyltransferase. J. Biol. Chem. 243 (1968) 6520–6528. [PMID: 5726897] |
2. |
Hickman, J., Ashwell, G., Morell, A.G., van der Hamer, C.J.A. and Scheinberg, I.H. Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin. J. Biol. Chem. 245 (1970) 759–766. [PMID: 4313609] |
3. |
Bartholomew, B.A., Jourdian, G.W. and Roseman, S. The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum. J. Biol. Chem. 248 (1973) 5751–5762. [PMID: 4723915] |
4. |
Paulson, J.C., Beranek, W.E. and Hill, R.L. Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose. J. Biol. Chem. 252 (1977) 2356–2362. [PMID: 849932] |
5. |
Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476] |
6. |
Albarracin, I., Lassaga, F.E. and Caputto, R. Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide α2,6-N-acetylneuraminyltransferase (EC 2.4.99.-). Biochem. J. 254 (1988) 559–565. [PMID: 2460092] |
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[EC 2.4.3.1 created 1972 as EC 2.4.99.1, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2016), modified 2017, transferred 2021 to EC 2.4.3.1] |
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EC |
1.14.99.63 | Relevance: 92.1% |
Accepted name: |
β-carotene 4-ketolase |
Reaction: |
(1) β-carotene + 2 reduced acceptor + 2 O2 = echinenone + 2 acceptor + 3 H2O (2) echinenone + 2 reduced acceptor + 2 O2 = canthaxanthin + 2 acceptor + 3 H2O |
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For diagram of canthaxanthin biosynthesis, click here |
Glossary: |
echinenone = β,β-caroten-4-one
canthaxanthin = β,β-carotene-4,4′-dione
zeaxanthin = β,β-carotene-3,3′-diol
astaxanthin = 3,3′-dihydroxy-β,β-carotene-4,4′-dione |
Other name(s): |
BKT (ambiguous); β-C-4 oxygenase; β-carotene ketolase; crtS (gene name); crtW (gene name) |
Systematic name: |
β-carotene,donor:oxygen oxidoreductase (echinenone-forming) |
Comments: |
The enzyme, studied from algae, plants, fungi, and bacteria, adds an oxo group at position 4 of a carotenoid β ring. It is involved in the biosynthesis of carotenoids such as astaxanthin and flexixanthin. The enzyme does not act on β rings that are hydroxylated at position 3, such as in zeaxanthin (cf. EC 1.14.99.64, zeaxanthin 4-ketolase). The enzyme from the yeast Xanthophyllomyces dendrorhous is bifuntional and also catalyses the activity of EC 1.14.15.24, β-carotene 3-hydroxylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Lotan, T. and Hirschberg, J. Cloning and expression in Escherichia coli of the gene encoding β-C-4-oxygenase, that converts β-carotene to the ketocarotenoid canthaxanthin in Haematococcus pluvialis. FEBS Lett. 364 (1995) 125–128. [PMID: 7750556] |
2. |
Breitenbach, J., Misawa, N., Kajiwara, S. and Sandmann, G. Expression in Escherichia coli and properties of the carotene ketolase from Haematococcus pluvialis. FEMS Microbiol. Lett. 140 (1996) 241–246. [PMID: 8764486] |
3. |
Steiger, S. and Sandmann, G. Cloning of two carotenoid ketolase genes from Nostoc punctiforme for the heterologous production of canthaxanthin and astaxanthin. Biotechnol. Lett. 26 (2004) 813–817. [PMID: 15269553] |
4. |
Ojima, K., Breitenbach, J., Visser, H., Setoguchi, Y., Tabata, K., Hoshino, T., van den Berg, J. and Sandmann, G. Cloning of the astaxanthin synthase gene from Xanthophyllomyces dendrorhous (Phaffia rhodozyma) and its assignment as a β-carotene 3-hydroxylase/4-ketolase. Mol. Genet. Genomics 275 (2006) 148–158. [PMID: 16416328] |
5. |
Tao, L., Yao, H., Kasai, H., Misawa, N. and Cheng, Q. A carotenoid synthesis gene cluster from Algoriphagus sp. KK10202C with a novel fusion-type lycopene β-cyclase gene. Mol. Genet. Genomics 276 (2006) 79–86. [PMID: 16625353] |
6. |
Kathiresan, S., Chandrashekar, A., Ravishankar, G.A. and Sarada, R. Regulation of astaxanthin and its intermediates through cloning and genetic transformation of β-carotene ketolase in Haematococcus pluvialis. J. Biotechnol. 196-197 (2015) 33–41. [PMID: 25612872] |
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[EC 1.14.99.63 created 2018] |
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EC |
5.5.1.17 | Relevance: 92% |
Accepted name: |
(S)-β-macrocarpene synthase |
Reaction: |
(S)-β-bisabolene = (S)-β-macrocarpene |
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For diagram of biosynthesis of bicyclic sesquiterpenoids derived from bisabolyl cation, click here and for diagram of bisabolene and macrocarpene biosynthesis, click here |
Other name(s): |
TPS6; TPS11; (S)-β-macrocarpene lyase (decyclizing) |
Systematic name: |
(S)-β-macrocarpene lyase (ring-opening) |
Comments: |
The synthesis of (S)-β-macrocarpene from (2E,6E)-farnesyl diphosphate proceeds in two steps. The first step is the cyclization to (S)-β-bisabolene (cf. EC 4.2.3.55, (S)-β-bisabolene synthase). The second step is the isomerization to (S)-β-macrocarpene. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kollner, T.G., Schnee, C., Li, S., Svatos, A., Schneider, B., Gershenzon, J. and Degenhardt, J. Protonation of a neutral (S)-β-bisabolene intermediate is involved in (S)-β-macrocarpene formation by the maize sesquiterpene synthases TPS6 and TPS11. J. Biol. Chem. 283 (2008) 20779–20788. [DOI] [PMID: 18524777] |
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[EC 5.5.1.17 created 2011] |
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EC |
2.4.1.134 | Relevance: 91.8% |
Accepted name: |
galactosylxylosylprotein 3-β-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + [protein]-3-O-(β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine = UDP + [protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine |
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For diagram of heparan and chondroitin biosynthesis (early stages), click here |
Other name(s): |
galactosyltransferase II; uridine diphosphogalactose-galactosylxylose galactosyltransferase; UDP-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase; UDP-α-D-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase |
Systematic name: |
UDP-α-D-galactose:[protein]-3-O-(β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine (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, CAS registry number: 56626-21-2, 56626-19-8 |
References: |
1. |
Robinson, J.A. and Robinson, H.C. Initiation of chondroitin sulphate synthesis by β-D-galactosides. Substrates for galactosyltransferase II. Biochem. J. 227 (1985) 805–814. [PMID: 3924029] |
2. |
Schwartz, N.B. and Roden, L. Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase. J. Biol. Chem. 250 (1975) 5200–5207. [PMID: 1150655] |
3. |
Bai, X., Zhou, D., Brown, J.R., Crawford, B.E., Hennet, T. and Esko, J.D. Biosynthesis of the linkage region of glycosaminoglycans: cloning and activity of galactosyltransferase II, the sixth member of the β1,3-galactosyltransferase family (β3GalT6). J. Biol. Chem. 276 (2001) 48189–48195. [DOI] [PMID: 11551958] |
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[EC 2.4.1.134 created 1984, modified 2002] |
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EC |
2.4.2.25 | Relevance: 91.6% |
Accepted name: |
flavone apiosyltransferase |
Reaction: |
UDP-α-D-apiose + apigenin 7-O-β-D-glucoside = UDP + apigenin 7-O-[β-D-apiosyl-(1→2)-β-D-glucoside] |
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For diagram of apigenin derivatives biosynthesis, click here |
Glossary: |
apigenin = 4′,5,7-trihydroxyflavone
β-D-apiose = (2R,3R,4R)-4-(hydroxymethyl)tetrahydrofuran-2,3,4-triol |
Other name(s): |
uridine diphosphoapiose-flavone apiosyltransferase; UDP-apiose:7-O-(β-D-glucosyl)-flavone apiosyltransferase |
Systematic name: |
UDP-apiose:5,4′-dihydroxyflavone 7-O-β-D-glucoside 2′′-O-β-D-apiofuranosyltransferase |
Comments: |
7-O-β-D-Glucosides of a number of flavonoids and of 4-substituted phenols can act as acceptors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37332-49-3 |
References: |
1. |
Ortmann, R., Sutter, A. and Grisebach, H. Purification and properties of UDPapiose: 7-O-(β-D-glucosyl)-flavone apiosyltransferase from cell suspension cultures of parsley. Biochim. Biophys. Acta 289 (1972) 293–302. [DOI] [PMID: 4650134] |
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[EC 2.4.2.25 created 1976] |
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EC |
5.4.99.62 | Relevance: 91.6% |
Accepted name: |
D-ribose pyranase |
Reaction: |
β-D-ribopyranose = β-D-ribofuranose |
Other name(s): |
RbsD |
Systematic name: |
D-ribopyranose furanomutase |
Comments: |
The enzyme also catalyses the conversion between β-allopyranose and β-allofuranose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kim, M.S., Shin, J., Lee, W., Lee, H.S. and Oh, B.H. Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture. J. Biol. Chem. 278 (2003) 28173–28180. [DOI] [PMID: 12738765] |
2. |
Ryu, K.S., Kim, C., Kim, I., Yoo, S., Choi, B.S. and Park, C. NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration. J. Biol. Chem. 279 (2004) 25544–25548. [DOI] [PMID: 15060078] |
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[EC 5.4.99.62 created 2014] |
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EC |
2.3.1.173 | Relevance: 91% |
Accepted name: |
flavonol-3-O-triglucoside O-coumaroyltransferase |
Reaction: |
4-coumaroyl-CoA + a flavonol 3-O-[β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside] = CoA + a flavonol 3-O-[6-(4-coumaroyl)-β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside] |
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For diagram of kaempferol-glycoside biosynthesis, click here |
Other name(s): |
4-coumaroyl-CoA:flavonol-3-O-[β-D-glucosyl-(1→2)-β-D-glucoside] 6′′′-O-4-coumaroyltransferase (incorrect) |
Systematic name: |
4-coumaroyl-CoA:flavonol 3-O-[β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside] 6′′′-O-4-coumaroyltransferase |
Comments: |
Acylates kaempferol 3-O-triglucoside on the terminal glucosyl unit, almost certainly at C-6. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64972-79-8 |
References: |
1. |
Saylor, M.H. and Mansell, R.L. Hydroxycinnamoyl:coenzyme A transferase involved in the biosynthesis of kaempferol-3-(p-coumaroyl triglucoside) in Pisum sativum. Z. Naturforsch. 32 (1977) 765–768. [PMID: 145116] |
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[EC 2.3.1.173 created 2004] |
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EC |
2.4.1.392 | Relevance: 90.9% |
Accepted name: |
3-O-β-D-glucopyranosyl-β-D-glucuronide phosphorylase |
Reaction: |
a 3-O-β-D-glucosyl-β-D-glucuronoside + phosphate = a β-D-glucuronoside + α-D-glucopyranose 1-phosphate |
Other name(s): |
PBOR_13355 (locus name) |
Systematic name: |
3-O-β-D-glucopyranosyl-β-D-glucuronide:phosphate α-D-glucosyltransferase |
Comments: |
The enzyme, characterized from the bacterium Paenibacillus borealis, catalyses a reversible reaction, transferring a glucosyl residue attached by a β(1,3) linkage to a D-glucuronate residue (either free or as a part of a β-D-glucuronide) to a free phosphate, generating α-D-glucopyranose 1-phosphate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Isono, N., Mizutani, E., Hayashida, H., Katsuzaki, H. and Saburi, W. Functional characterization of a novel GH94 glycoside phosphorylase, 3-O-β-D-glucopyranosyl β-D-glucuronide phosphorylase, and implication of the metabolic pathway of acidic carbohydrates in Paenibacillus borealis. Biochem. Biophys. Res. Commun. 625 (2022) 60–65. [DOI] [PMID: 35947916] |
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[EC 2.4.1.392 created 2022] |
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EC |
3.2.1.164 | Relevance: 90.7% |
Accepted name: |
galactan endo-1,6-β-galactosidase |
Reaction: |
Endohydrolysis of (1→6)-β-D-galactosidic linkages in arabinogalactan proteins and (1→3):(1→6)-β-galactans to yield galactose and (1→6)-β-galactobiose as the final products |
Other name(s): |
endo-1,6-β-galactanase |
Systematic name: |
endo-β-(1→6)-galactanase |
Comments: |
The enzyme specifically hydrolyses 1,6-β-D-galactooligosaccharides with a degree of polymerization (DP) higher than 3, and their acidic derivatives with 4-O-methylglucosyluronate or glucosyluronate groups at the non-reducing terminals [2]. 1,3-β-D- and 1,4-β-D-galactosyl residues cannot act as substrates. The enzyme can also hydrolyse α-L-arabinofuranosidase-treated arabinogalactan protein (AGP) extracted from radish roots [2,3]. AGPs are thought to be involved in many physiological events, such as cell division, cell expansion and cell death [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Brillouet, J.-M., Williams, P. and Moutounet, M. Purification and some properties of a novel endo-β-(1→6)-D-galactanase from Aspergillus niger. Agric. Biol. Chem. 55 (1991) 1565–1571. |
2. |
Okemoto, K., Uekita, T., Tsumuraya, Y., Hashimoto, Y. and Kasama, T. Purification and characterization of an endo-β-(1→6)-galactanase from Trichoderma viride. Carbohydr. Res. 338 (2003) 219–230. [DOI] [PMID: 12543554] |
3. |
Kotake, T., Kaneko, S., Kubomoto, A., Haque, M.A., Kobayashi, H. and Tsumuraya, Y. Molecular cloning and expression in Escherichia coli of a Trichoderma viride endo-β-(1→6)-galactanase gene. Biochem. J. 377 (2004) 749–755. [DOI] [PMID: 14565843] |
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[EC 3.2.1.164 created 2007] |
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EC |
2.4.1.274 | Relevance: 90.7% |
Accepted name: |
glucosylceramide β-1,4-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
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For diagram of glycolipid biosynthesis, click here |
Other name(s): |
lactosylceramide synthase; uridine diphosphate-galactose:glucosyl ceramide β 1-4 galactosyltransferase; UDP-Gal:glucosylceramide β1→4galactosyltransferase; GalT-2 (misleading); UDP-galactose:β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase |
Systematic name: |
UDP-α-D-galactose:β-D-glucosyl-(1↔1)-ceramide 4-β-D-galactosyltransferase |
Comments: |
Involved in the synthesis of several different major classes of glycosphingolipids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Chatterjee, S. and Castiglione, E. UDPgalactose:glucosylceramide β1→4-galactosyltransferase activity in human proximal tubular cells from normal and familial hypercholesterolemic homozygotes. Biochim. Biophys. Acta 923 (1987) 136–142. [DOI] [PMID: 3099851] |
2. |
Trinchera, M., Fiorilli, A. and Ghidoni, R. Localization in the Golgi apparatus of rat liver UDP-Gal:glucosylceramide β1→4galactosyltransferase. Biochemistry 30 (1991) 2719–2724. [PMID: 1900430] |
3. |
Chatterjee, S., Ghosh, N. and Khurana, S. Purification of uridine diphosphate-galactose:glucosyl ceramide, β 1-4 galactosyltransferase from human kidney. J. Biol. Chem. 267 (1992) 7148–7153. [PMID: 1551920] |
4. |
Nomura, T., Takizawa, M., Aoki, J., Arai, H., Inoue, K., Wakisaka, E., Yoshizuka, N., Imokawa, G., Dohmae, N., Takio, K., Hattori, M. and Matsuo, N. Purification, cDNA cloning, and expression of UDP-Gal: glucosylceramide β-1,4-galactosyltransferase from rat brain. J. Biol. Chem. 273 (1998) 13570–13577. [DOI] [PMID: 9593693] |
5. |
Takizawa, M., Nomura, T., Wakisaka, E., Yoshizuka, N., Aoki, J., Arai, H., Inoue, K., Hattori, M. and Matsuo, N. cDNA cloning and expression of human lactosylceramide synthase. Biochim. Biophys. Acta 1438 (1999) 301–304. [DOI] [PMID: 10320813] |
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[EC 2.4.1.274 created 2011] |
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EC |
3.4.24.32 | Relevance: 90.4% |
Accepted name: |
β-lytic metalloendopeptidase |
Reaction: |
Cleavage of N-acetylmuramoyl┼Ala, and of the insulin B chain at Gly23┼Phe > Val18┼Cya |
Other name(s): |
Myxobacter β-lytic proteinase; achromopeptidase component; β-lytic metalloproteinase; β-lytic protease; Myxobacterium sorangium β-lytic proteinase; Myxobacter495 β-lytic proteinase |
Comments: |
From Achromobacter lyticus and Lysobacter enzymogenes. Digests bacterial cell walls. Type example of peptidase family M23. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 37288-92-9 |
References: |
1. |
Whitaker, D.R., Roy, C., Tsai, C.S. and Juraöek, L. Lytic enzymes of Sorangium sp. A comparison of the proteolytic properties of the α- and β-lytic proteases. Can. J. Biochem. 43 (1965) 1961–1970. [PMID: 5880182] |
2. |
Whitaker, D.R. and Roy, C. Concerning the nature of the α- and β-lytic proteases of Sorangium sp. Can. J. Biochem. 45 (1967) 911. [PMID: 6034704] |
3. |
Li, S. L., Norioka, S. and Sakiyama, F. Molecular cloning and nucleotide sequence of the β-lytic protease gene from Achromobacter lyticus. J. Bacteriol. 172 (1990) 6506–6511. [DOI] [PMID: 2228973] |
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[EC 3.4.24.32 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.32] |
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EC |
5.1.3.44 | Relevance: 90.3% |
Accepted name: |
mannose 2-epimerase |
Reaction: |
β-D-mannopyranose = β-D-glucopyranose |
Systematic name: |
β-D-mannopyranose 2-epimerase |
Comments: |
The enzyme, characterized from multiple bacterial species, catalyses the interconversion between β-D-glucopyranose and β-D-mannopyranose through proton abstraction-addition at the C2 position. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Saburi, W., Sato, S., Hashiguchi, S., Muto, H., Iizuka, T. and Mori, H. Enzymatic characteristics of D-mannose 2-epimerase, a new member of the acylglucosamine 2-epimerase superfamily. Appl. Microbiol. Biotechnol. 103 (2019) 6559–6570. [DOI] [PMID: 31201453] |
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[EC 5.1.3.44 created 2020] |
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