The Enzyme Database

Displaying entries 101-150 of 1139.

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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]
 
 
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]
 
 
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]
 
 
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]
 
 
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]
 
 
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]
[EC 2.4.1.179 created 1989]
 
 
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.
[EC 3.4.19.5 created 1972 as EC 3.4.13.10, transferred 1992 to EC 3.4.19.5, modified 1997]
 
 
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]
 
 
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]
 
 
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]
 
 
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]
[EC 3.2.1.197 created 2016]
 
 
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]
 
 
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]
 
 
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]
[EC 3.2.1.58 created 1972]
 
 
EC 1.13.12.12      
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
[EC 1.13.12.12 created 2000, modified 2001, deleted 2012]
 
 
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]
[EC 3.2.1.185 created 2013]
 
 
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
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]
[EC 2.4.1.275 created 2011, modified 2013]
 
 
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.
[EC 3.2.1.43 created 1972]
 
 
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
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]
[EC 3.2.1.154 created 2005]
 
 
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.
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]
[EC 3.2.1.181 created 2012]
 
 
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
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]
[EC 2.4.1.249 created 2009]
 
 
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]
[EC 2.4.1.38 created 1972, modified 1976, modified 1980, modified 1986]
 
 
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.
[EC 3.2.1.4 created 1961, modified 2001]
 
 
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]
[EC 3.2.1.145 created 2001]
 
 
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]
[EC 3.2.1.53 created 1972]
 
 
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]
[EC 3.2.1.146 created 2001]
 
 
EC 2.4.99.2      
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
[EC 2.4.99.2 created 1976, modified 1986, deleted 2022]
 
 
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
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]
[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]
 
 
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]
[EC 3.2.1.92 created 1976]
 
 
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]
[EC 3.2.1.26 created 1961]
 
 
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]
[EC 3.2.1.214 created 2020]
 
 
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]
[EC 1.13.11.67 created 2000 as EC 1.13.12.12, transferred 2012 to EC 1.13.11.67]
 
 
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]
[EC 2.4.1.27 created 1965]
 
 
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]
[EC 3.2.1.71 created 1972]
 
 
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]
[EC 3.2.1.31 created 1961]
 
 
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.
[EC 1.5.1.26 created 1990]
 
 
EC 2.4.99.1      
Transferred entry: β-galactoside α-(2,6)-sialyltransferase. Now EC 2.4.3.1, β-galactoside α-(2,6)-sialyltransferase
[EC 2.4.99.1 created 1972, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2017), deleted 2022]
 
 
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]
[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]
 
 
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
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]
[EC 1.14.99.63 created 2018]
 
 
EC 5.5.1.17     Relevance: 92%
Accepted name: (S)-β-macrocarpene synthase
Reaction: (S)-β-bisabolene = (S)-β-macrocarpene
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]
[EC 5.5.1.17 created 2011]
 
 
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
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]
[EC 2.4.1.134 created 1984, modified 2002]
 
 
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]
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]
[EC 2.4.2.25 created 1976]
 
 
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]
[EC 5.4.99.62 created 2014]
 
 
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]
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]
[EC 2.3.1.173 created 2004]
 
 
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]
[EC 2.4.1.392 created 2022]
 
 
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]
[EC 3.2.1.164 created 2007]
 
 
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
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]
[EC 2.4.1.274 created 2011]
 
 
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]
[EC 3.4.24.32 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.32]
 
 
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]
[EC 5.1.3.44 created 2020]
 
 


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