Enzyme Nomenclature

EC 3.2.1 (continued)

Hydrolysing O-Glycosyl Compounds

See separate file for EC 3.2.1.1 to EC 3.2.1.50, EC 3.2.1.51 to EC 3.2.1.100 and EC 3.2.1.151 to EC 3.2.1.208.

Contents

EC 3.2.1.101 mannan endo-1,6-α-mannosidase
EC 3.2.1.102 blood-group-substance endo-1,4-β-galactosidase
EC 3.2.1.103 keratan-sulfate endo-1,4-β-galactosidase
EC 3.2.1.104 steryl-β-glucosidase
EC 3.2.1.105 strictosidine β-glucosidase
EC 3.2.1.106 mannosyl-oligosaccharide glucosidase
EC 3.2.1.107 protein-glucosylgalactosylhydroxylysine glucosidase
EC 3.2.1.108 lactase
EC 3.2.1.109 endogalactosaminidase
EC 3.2.1.110 deleted identical to EC 3.2.1.97
EC 3.2.1.111 1,3-α-L-fucosidase
EC 3.2.1.112 2-deoxyglucosidase
EC 3.2.1.113 mannosyl-oligosaccharide 1,2-α-mannosidase
EC 3.2.1.114 mannosyl-oligosaccharide 1,3-1,6-α-mannosidase
EC 3.2.1.115 branched-dextran exo-1,2-α-glucosidase
EC 3.2.1.116 glucan 1,4-α-maltotriohydrolase
EC 3.2.1.117 amygdalin β-glucosidase
EC 3.2.1.118 prunasin β-glucosidase
EC 3.2.1.119 vicianin β-glucosidase
EC 3.2.1.120 oligoxyloglucan β-glycosidase
EC 3.2.1.121 polymannuronate hydrolase
EC 3.2.1.122 maltose-6'-phosphate glucosidase
EC 3.2.1.123 endoglycosylceramidase
EC 3.2.1.124 3-deoxy-2-octulosonidase
EC 3.2.1.125 raucaffricine β-glucosidase
EC 3.2.1.126 coniferin β-glucosidase
EC 3.2.1.127 1,6-α-L-fucosidase
EC 3.2.1.128 glycyrrhizinate β-glucuronidase
EC 3.2.1.129 endo-α-sialidase
EC 3.2.1.130 glycoprotein endo-α-1,2-mannosidase
EC 3.2.1.131 xylan α-1,2-glucuronosidase
EC 3.2.1.132 chitosanase
EC 3.2.1.133 glucan 1,4-α-maltohydrolase
EC 3.2.1.134 difructose-anhydride synthase
EC 3.2.1.135 neopullulanase
EC 3.2.1.136 glucuronoarabinoxylan endo-1,4-β-xylanase
EC 3.2.1.137 mannan exo-1,2-1,6-α-mannosidase
EC 3.2.1.138 now EC 4.2.2.15
EC 3.2.1.139 α-glucuronidase
EC 3.2.1.140 lacto-N-biosidase
EC 3.2.1.141 4-α-D-{(1→4)-α-D-glucano}trehalose trehalohydrolase
EC 3.2.1.142 limit dextrinase
EC 3.2.1.143 poly(ADP-ribose) glycohydrolase
EC 3.2.1.144 3-deoxyoctulosonase
EC 3.2.1.145 galactan 1,3-β-galactosidase
EC 3.2.1.146 β-galactofuranosidase
EC 3.2.1.147 thioglucosidase
EC 3.2.1.148 now EC 4.4.1.21
EC 3.2.1.149 β-primeverosidase
EC 3.2.1.150 oligoxyloglucan reducing-end-specific cellobiohydrolase

See the following file for:

EC 3.2.1.151 to EC 3.2.1.208

Entries

EC 3.2.1.101

Accepted name: mannan endo-1,6-α-mannosidase

Reaction: Random hydrolysis of (1→6)-α-D-mannosidic linkages in unbranched (1→6)-mannans

Other name(s): endo-α-1→6-D-mannanase; endo-1,6-β-mannanase; mannan endo-1,6-β-mannosidase; 1,6-α-D-mannan mannanohydrolase

Systematic name: 6-α-D-mannan mannanohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 58500-56-4

References:

1. Nakajima, T., Maitra, S.K. and Ballou, C.E. An endo-α-1→6-D-mannanase from a soil bacterium. Purification, properties, and mode of action. J. Biol. Chem. 251 (1976) 174-181. [PMID: 811665]

2. Brigance, W.T., Barlowe, C. and Graham, T.R. Organization of the yeast Golgi complex into at least four functionally distinct compartments. Mol. Biol. Cell 11 (2000) 171-182. [PMID: 10637300]

3. Nakajima, T. and Ballou, C.E. Structure of the linkage region between the polysaccharide and protein parts of Saccharomyces cerevisiae mannan. J. Biol. Chem. 249 (1974) 7685-7694. [PMID: 4612041]

[EC 3.2.1.101 created 1984, modified 2001]

EC 3.2.1.102

Accepted name: blood-group-substance endo-1,4-β-galactosidase

Reaction: Endohydrolysis of (1→4)-β-D-galactosidic linkages in blood group A and B substances

Other name(s): endo-β-galactosidase (ambiguous); blood-group-substance 1,4-β-D-galactanohydrolase

Systematic name: blood-group-substance 4-β-D-galactanohydrolase

Comments: Hydrolyses the 1,4-β-D-galactosyl linkages adjacent to a 1,3-α-D-galactosyl or N-acetylgalactosaminyl residues and a 1,2-α-D-fucosyl residue.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52720-51-1

References:

1. Fukuda, M.N. and Matsumara, G. Endo-β-galactosidase of Escherichia freundii. Purification and endoglycosidic action on keratan sulfates, oligosaccharides, and blood group active glycoprotein. J. Biol. Chem. 251 (1976) 6218-6225. [PMID: 135762]

2. Nakazawa, K. and Suzuki, S. Purification of keratan sulfate-endogalactosidase and its action on keratan sulfates of different origin. J. Biol. Chem. 250 (1975) 912-917. [PMID: 234443]

3. Takasaki, S. and Kobata, A. Purification and characterization of an endo-β-galactosidase produced by Diplococcus pneumoniae. J. Biol. Chem. 251 (1976) 3603-3609. [PMID: 6459]

[EC 3.2.1.102 created 1984]

EC 3.2.1.103

Accepted name: keratan-sulfate endo-1,4-β-galactosidase

Reaction: Endohydrolysis of (1→4)-β-D-galactosidic linkages in keratan sulfate

Other name(s): endo-β-galactosidase (ambiguous); keratan sulfate endogalactosidase; keratanase; keratan-sulfate 1,4-β-D-galactanohydrolase

Systematic name: keratan-sulfate 4-β-D-galactanohydrolase

Comments: Hydrolyses the 1,4-β-D-galactosyl linkages adjacent to 1,3-N-acetyl-α-D-glucosaminyl residues. Also acts on some non-sulfated oligosaccharides, but only acts on blood group substances when the 1,2-linked fucosyl residues have been removed (cf. EC 3.2.1.102 blood-group-substance endo-1,4-β-galactosidase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 55072-01-0

References:

1. Fukuda, M.N. and Matsumara, G. Endo-β-galactosidase of Escherichia freundii. Purification and endoglycosidic action on keratan sulfates, oligosaccharides, and blood group active glycoprotein. J. Biol. Chem. 251 (1976) 6218-6225. [PMID: 135762]

[EC 3.2.1.103 created 1984]

EC 3.2.1.104

Accepted name: steryl-β-glucosidase

Reaction: cholesteryl-β-D-glucoside + H2O = D-glucose + cholesterol

Systematic name: cholesteryl-β-D-glucoside glucohydrolase

Comments: Acts on glucosides of cholesterol and sitosterol, but not on some related sterols such as coprostanol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 69494-88-8

References:

1. Kalinowska, M. and Wojciechowski, Z.A. Purification and some properties of steryl β-D-glucoside hydrolase from Sinapis alba seedlings. Phytochemistry 17 (1978) 1533-1537.

[EC 3.2.1.104 created 1984]

EC 3.2.1.105

Accepted name: 3α(S)-strictosidine β-glucosidase

Reaction: strictosidine + H2O = D-glucose + strictosidine aglycone

For diagram click here.

Systematic name: strictosidine β-D-glucohydrolase

Comments: Does not act on a number of closely related glycosides. Strictosidine is a precursor of indole alkaloids.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 73379-57-4

References:

1. Hemscheidt, T. and Zenk, M.H. Glucosidases involved in indole alkaloid biosynthesis of Catharanthus cell cultures. FEBS Lett. 110 (1980) 187-191. [PMID: 6768587]

2. Barleben, L., Ma, X., Koepke, J., Peng, G., Michel, H. and Stöckigt, J. Expression, purification, crystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to a unique diversity of indole alkaloid skeletons. Biochim. Biophys. Acta 1747 (2005) 89-92. [PMID: 15680242]

[EC 3.2.1.105 created 1984]

EC 3.2.1.106

Accepted name: mannosyl-oligosaccharide glucosidase

Reaction: Glc3Man9GlcNAc2-[protein] + H2O = Glc2Man9GlcNAc2-[protein] + β-D-glucopyranose

Glossary: Glc3Man9GlcNAc2 = [α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Glc2Man9GlcNAc2-[protein] = [α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]

Other name(s): Glc3Man9NAc2 oligosaccharide glucosidase; trimming glucosidase I; CWH41 (gene name); MOGS (gene name); mannosyl-oligosaccharide glucohydrolase

Systematic name: Glc3Man9GlcNAc2-[protein] glucohydrolase (configuration-inverting)

Comments: This enzyme catalyses the first step in the processing of the N-glycan tetradecasaccharide precursor Glc3Man9GlcNAc2, which takes place in the endoplasmic reticulum, by removing the distal α-1,2-linked glucose residue. This and subsequent processing steps are required before complex N-glycans can be synthesized.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 78413-07-7

References:

1. Elting, J.J., Chen, W.W. and Lennarz, J. Characterization of a glucosidase involved in an initial step in the processing of oligosaccharide chains. J. Biol. Chem. 255 (1980) 2325-2331. [PMID: 7358674]

2. Grinna, L.S. and Robbins, P.W. Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides. J. Biol. Chem. 254 (1979) 8814-8818. [PMID: 479161]

3. Kilker, R.D., Saunier, B., Tkacz, J.S. and Herscovics, A. Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2. J. Biol. Chem. 256 (1981) 5299-5603. [PMID: 7014569]

4. Grinna, L.S. and Robbins, P.W. Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J. Biol. Chem. 255 (1980) 2255-2258. [PMID: 7358666]

5. Mark, M.J. and Kornfeld, S. Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides. Arch. Biochem. Biophys. 199 (1980) 249-258. [PMID: 7356331]

[EC 3.2.1.106 created 1984, modified 2018]

EC 3.2.1.107

Accepted name: protein-glucosylgalactosylhydroxylysine glucosidase

Reaction: protein α-D-glucosyl-(1→2)-β-D-galactosyl-L-hydroxylysine + H2O = D-glucose + protein β-D-galactosyl-L-hydroxylysine

Other name(s): 2-O-α-D-glucopyranosyl-5-O-α-D-galactopyranosylhydroxy-L-lysine glucohydrolase; protein-α-D-glucosyl-1,2-β-D-galactosyl-L-hydroxylysine glucohydrolase

Systematic name: protein-α-D-glucosyl-(1→2)-β-D-galactosyl-L-hydroxylysine glucohydrolase

Comments: Requires free, positively charged ε-amino group of hydroxylysine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72829-45-9

References:

1. Hamazaki, H. and Hotta, K. Purification and characterization of an α-glucosidase specific for hydroxylysine-linked disaccharide of collagen. J. Biol. Chem. 254 (1979) 9682-9687. [PMID: 385589]

2. Hamazaki, H. and Hotta, K. Enzymatic hydrolysis of disaccharide unit of collagen. Isolation of 2-O-α-D-glucopyranosyl-O-β-D-galactopyranosyl-hydroxylysine glucohydrolase from rat spleens. Eur. J. Biochem. 111 (1980) 587-591. [PMID: 7460918]

3. Sternberg, M. and Shapiro, R.G. Studies on the catabolism of the hydroxylysine-linked disaccharide units of basement membranes and collagens. Isolation and characterization of a rat kidney α-glucosidase of high specificity. J. Biol. Chem. 254 (1979) 10329-10336. [PMID: 385599]

[EC 3.2.1.107 created 1984]

EC 3.2.1.108

Accepted name: lactase

Reaction: lactose + H2O = D-galactose + D-glucose

Glossary: lactose = β-D-galactopyranosyl-(1→4)-α-D-glucopyranose

Other name(s): lactase-phlorizin hydrolase

Systematic name: lactose galactohydrolase

Comments: The enzyme from intestinal mucosa is isolated as a complex that also catalyses the reaction of EC 3.2.1.62 glycosylceramidase. cf. EC 3.2.1.33 amylo-α-1,6-glucosidase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9031-11-2

References:

1. Lorenz-Meyer, H., Blum, A.L., Haemmerli, H.P. and Semenza, G. Second enzyme defect in lactase deficiency. Lack of small-intestinal phlorizin-hydrolase. Eur. J. Clin. Invest. 2 (1972) 326-331. [PMID: 5082068]

2. Ramaswamay, S. and Radhakrishnan, A.N. Lactase-phlorizin hydrolase complex from monkey small intestine. Purification, properties and evidence for two catalytic sites. Biochim. Biophys. Acta 403 (1975) 446-455. [PMID: 810166]

3. Schlegel-Haueter, S., Hore, P., Kerry, K.R. and Semenza, G. The preparation of lactase and glucoamylase of rat small intestine. Biochim. Biophys. Acta 258 (1972) 506-519. [PMID: 5010299]

4. Skovbjerg, H., Norén, O., Sjöström, H., Danielsen, E.M. and Enevoldsen, B.S. Further characterization of intestinal lactase/phlorizin hydrolase. Biochim. Biophys. Acta 707 (1982) 89-97. [PMID: 6814489]

5. Skovbjerg, H., Sjöström, H. and Norén, O. Purification and characterization of amphiphilic lactase-phlorizin hydrolase from human small-intestine. Eur. J. Biochem. 114 (1981) 653-661. [PMID: 6786877]

6. Asp, N.G., Dahlqvist, A. and Koldovský, O. Human small-intestinal β-galactosidases. Separation and characterization of one lactase and one hetero β-galactosidase. Biochem. J. 114 (1969) 351-359. [PMID: 5822067]

[EC 3.2.1.108 created 1984]

EC 3.2.1.109

Accepted name: endogalactosaminidase

Reaction: Endohydrolysis of (1→4)-α-D-galactosaminidic linkages in poly(D-galactosamine)

Systematic name: galactosaminoglycan glycanohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 118478-30-1

References:

1. Reissig, J.L., Lau, W. and Glasgow, J.E. An endogalactosaminidase from Streptomyces griseus. Can. J. Biochem. 53 (1975) 1237-1249. [PMID: 3271]

2. Tamura, J., Takagi, H. and Kadowaki, K. Purification and some properties of the endo α-1,4-polygalactosaminidase from Pseudomonas sp. Agric. Biol. Chem. 52 (1988) 2475-2484.

[EC 3.2.1.109 created 1984]

[EC 3.2.1.110 Deleted entry: mucinaminylserine mucinaminidase. The enzyme is identical to EC 3.2.1.97, glycopeptide α-N-acetylgalactosaminidase (EC 3.2.1.110 created 1984, deleted 2008)]

EC 3.2.1.111

Accepted name: 1,3-α-L-fucosidase

Reaction: Hydrolysis of (1→3)-linkages between α-L-fucose and N-acetylglucosamine residues in glycoproteins

Other name(s): almond emulsin fucosidase I

Systematic name: 3-α-L-fucosyl-N-acetylglucosaminyl-glycoprotein fucohydrolase

Comments: Not identical with EC 3.2.1.63 1,2-α-L-fucosidase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 83061-50-1

References:

1. Imber, M.J., Glasgow, L.R. and Pizzo, S.V. Purification of an almond emulsin fucosidase on Cibacron blue-sepharose and demonstration of its activity toward fucose-containing glycoproteins. J. Biol. Chem. 257 (1982) 8205-8210. [PMID: 7085666]

2. Ogata-Arakawa, M., Muramatsu, T. and Kobata, A. α-L-Fucosidases from almond emulsin: characterization of the two enzymes with different specificities. Arch. Biochem. Biophys. 181 (1977) 353-358. [PMID: 18111]

3. Yoshima, H., Takasaki, S., Ito-Mega, S. and Kobata, A. Purification of almond emulsin α-L-fucosidase I by affinity chromatography. Arch. Biochem. Biophys. 194 (1979) 394-398. [PMID: 443810]

[EC 3.2.1.111 created 1986]

EC 3.2.1.112

Accepted name: 2-deoxyglucosidase

Reaction: a 2-deoxy-α-D-glucoside + H2O = 2-deoxy-D-glucose + an alcohol

Other name(s): 2-deoxy-α-glucosidase; 2-deoxy-α-D-glucosidase

Systematic name: 2-deoxy-α-D-glucoside deoxyglucohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 92480-05-2

References:

1. Canellakis, Z.N., Bondy, P.K., May, J.A., Jr., Myers-Robfogel, M.K. and Sartorelli, A.C. Identification of a glycosidase activity with apparent specificity for 2-deoxy-D-glucose in glycosidic linkage. Eur. J. Biochem. 143 (1984) 159-163. [PMID: 6468386]

[EC 3.2.1.112 created 1986]

EC 3.2.1.113

Accepted name: mannosyl-oligosaccharide 1,2-α-mannosidase

Reaction: Hydrolysis of the terminal (1→2)-linked α-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2

Other name(s): mannosidase 1A; mannosidase 1B; 1,2-α-mannosidase; exo-α-1,2-mannanase; mannose-9 processing α-mannosidase; glycoprotein processing mannosidase I; mannosidase I; Man9-mannosidase; ManI; 1,2-α-mannosyl-oligosaccharide α-D-mannohydrolase

Systematic name: 2-α-mannosyl-oligosaccharide α-D-mannohydrolase

Comments: Involved in the synthesis of glycoproteins.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9068-25-1

References:

1. Tabas, I. and Kornfeld, S. Purification and characterization of a rat liver Golgi α-mannosidase capable of processing asparagine-linked oligosaccharides. J. Biol. Chem. 254 (1979) 11655-11663. [PMID: 500665]

2. Tulsiani, D.R.P., Hubbard, S.C., Robbins, P.W. and Touster, O. α-D-Mannosidases of rat liver Golgi membranes. Mannosidase II is the GlcNAcMAN5-cleaving enzyme in glycoprotein biosynthesis and mannosidases Ia and IB are the enzymes converting Man9 precursors to Man5 intermediates. J. Biol. Chem. 257 (1982) 3660-3668. [PMID: 7061502]

[EC 3.2.1.113 created 1986]

EC 3.2.1.114

Accepted name: mannosyl-oligosaccharide 1,3-1,6-α-mannosidase

Reaction: Man5GlcNAc3-[protein] + 2 H2O = Man3GlcNAc3-[protein] + 2 α-D-mannopyranose

For diagram of reaction click here.

Glossary: Man5GlcNAc3-[protein] = [β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Man3GlcNAc3-[protein] = {β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-N-Asn-[protein]

Other name(s): MAN2A1 (gene name); MAN2A2 (gene name); mannosidase II; exo-1,3-1,6-α-mannosidase; α-D-mannosidase II; α-mannosidase II; α1-3,6-mannosidase; GlcNAc transferase I-dependent α1,3[α1,6]mannosidase; Golgi α-mannosidase II; ManII; 1,3(1,6)-α-D-mannosidase; 1,3-(1,6-)mannosyl-oligosaccharide α-D-mannohydrolase; (1→3)-(1→6)-mannosyl-oligosaccharide α-D-mannohydrolase

Systematic name: (1→3)-(1→6)-mannosyl-oligosaccharide α-D-mannohydrolase (configuration-retaining)

Comments: The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. It removes two mannosyl residues, one linked by α1,3 linkage, and the other linked by α1,6 linkage, both of which are removed by the same catalytic site. The enzyme is sensitive to swainsonine.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 82047-77-6

References:

1. Tulsiani, D.R.P., Opheim, D.J. and Touster, O. Purification and characterization of α-D-mannosidase from rat liver golgi membranes. J. Biol. Chem. 252 (1977) 3227-3233. [PMID: 863880]

2. Tabas, I. and Kornfeld, S. The synthesis of complex-type oligosaccharides. III. Identification of an α-D-mannosidase activity involved in a late stage of processing of complex-type oligosaccharides. J. Biol. Chem. 253 (1978) 7779-7786. [PMID: 212436]

3. Harpaz, N. and Schachter, H. Control of glycoprotein synthesis. Processing of asparagine-linked oligosaccharides by one or more rat liver Golgi α-D-mannosidases dependent on the prior action of UDP-N-acetylglucosamine: α-D-mannoside β2-N-acetylglucosaminyltransferase I. J. Biol. Chem. 255 (1980) 4894-4902. [PMID: 6445359]

4. Tulsiani, D.R.P., Hubbard, S.C., Robbins, P.W. and Touster, O. α-D-Mannosidases of rat liver Golgi membranes. Mannosidase II is the GlcNAcMAN5-cleaving enzyme in glycoprotein biosynthesis and mannosidases IA and IB are the enzymes converting Man9 precursors to Man5 intermediates. J. Biol. Chem. 257 (1982) 3660-3668. [PMID: 7061502]

5. Moremen, K.W. and Robbins, P.W. Isolation, characterization, and expression of cDNAs encoding murine α-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans. J. Cell Biol. 115 (1991) 1521-1534. [PMID: 1757461]

6. Misago, M., Liao, Y.F., Kudo, S., Eto, S., Mattei, M.G., Moremen, K.W. and Fukuda, M.N. Molecular cloning and expression of cDNAs encoding human α-mannosidase II and a previously unrecognized α-mannosidase IIx isozyme. Proc. Natl Acad. Sci. USA 92 (1995) 11766-11770. [PMID: 8524845]

7. van den Elsen, J.M., Kuntz, D.A. and Rose, D.R. Structure of Golgi α-mannosidase II: a target for inhibition of growth and metastasis of cancer cells. EMBO J. 20 (2001) 3008-3017. [PMID: 11406577]

8. Athanasopoulos, V.I., Niranjan, K. and Rastall, R.A. The production, purification and characterisation of two novel α-D-mannosidases from Aspergillus phoenicis. Carbohydr. Res. 340 (2005) 609-617. [PMID: 15721331]

9. Shah, N., Kuntz, D.A. and Rose, D.R. Golgi α-mannosidase II cleaves two sugars sequentially in the same catalytic site. Proc. Natl Acad. Sci. USA 105 (2008) 9570-9575. [PMID: 18599462]

10. Rose, D.R. Structure, mechanism and inhibition of Golgi α-mannosidase II. Curr. Opin. Struct. Biol. 22 (2012) 558-562. [PMID: 22819743]

[EC 3.2.1.114 created 1986, modified 2018]

EC 3.2.1.115

Accepted name: branched-dextran exo-1,2-α-glucosidase

Reaction: Hydrolysis of (1→2)-α-D-glucosidic linkages at the branch points of dextrans and related polysaccharides, producing free D-glucose

Other name(s): dextran 1,2-α-glucosidase; dextran α-1,2 debranching enzymel 1,2-α-D-glucosyl-branched-dextran 2-glucohydrolase

Systematic name: (1→2)-α-D-glucosyl-branched-dextran 2-glucohydrolase

Comments: Does not hydrolyse disaccharides or oligosaccharides containing linear 1,2-α-glucosidic linkages.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 72840-94-9

References:

1. Mitsuishi, Y., Kobayashi, M. and Matsuda, K. Dextran α-1,2-debranching enzyme from Flavobacterium sp. M-73: its production and purification. Agric. Biol. Chem. 43 (1979) 2283-2290.

2. Mitsuishi, Y., Kobayashi, M. and Matsuda, K. Dextran α-(1→2)-debranching enzyme from Flavobacterium sp. M-73. Properties and mode of action. Carbohydr. Res. 83 (1980) 303-313. [PMID: 7407800]

[EC 3.2.1.115 created 1989]

EC 3.2.1.116

Accepted name: glucan 1,4-α-maltotriohydrolase

Reaction: Hydrolysis of (1→4)-α-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotriose residues from the non-reducing chain ends

Other name(s): exo-maltotriohydrolase; maltotriohydrolase; 1,4-α-D-glucan maltotriohydrolase

Systematic name: 4-α-D-glucan maltotriohydrolase

Comments: cf. EC 3.2.1.2 (β-amylase), EC 3.2.1.60 (glucan 1,4-α-maltotetraohydrolase) and EC 3.2.1.98 (glucan 1,4-α-maltohexaosidase). The products have the α-configuration.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 91273-84-6

References:

1. Nakakuki, T., Azuma, K. and Kainuma, K. Action patterns of various exo-amylases and the anomeric configurations of their products. Carbohydr. Res. 128 (1984) 297-310.

[EC 3.2.1.116 created 1989]

EC 3.2.1.117

Accepted name: amygdalin β-glucosidase

Reaction: (R)-amygdalin + H2O = (R)-prunasin + D-glucose

Other name(s): amygdalase; amygdalinase; amygdalin hydrolase; amygdalin glucosidase

Systematic name: amygdalin β-D-glucohydrolase

Comments: Highly specific; does not act on prunasin, linamarin, gentiobiose or cellobiose (cf. EC 3.2.1.21 β-glucosidase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 51683-43-3

References:

1. Kuroki, G., Lizotte, P.A. and Poulton, J.E. L-β-Glycosidases from Prunus serotina EHRH and Davallia trichomanoides. Z. Natursforsch. C: Biosci. 39 (1984) 232-239.

[EC 3.2.1.117 created 1989]

EC 3.2.1.118

Accepted name: prunasin β-glucosidase

Reaction: (R)-prunasin + H2O = D-glucose + mandelonitrile

Other name(s): prunasin hydrolase

Systematic name: prunasin β-D-glucohydrolase

Comments: Highly specific; does not act on amygdalin, linamarin or gentiobiose. (cf. EC 3.2.1.21 β-glucosidase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9023-41-0

References:

1. Kuroki, G., Lizotte, P.A. and Poulton, J.E. L-β-Glycosidases from Prunus serotina EHRH and Davallia trichomanoides. Z. Natursforsch. C: Biosci. 39 (1984) 232-239.

[EC 3.2.1.118 created 1989]

EC 3.2.1.119

Accepted name: vicianin β-glucosidase

Reaction: (R)-vicianin + H2O = mandelonitrile + vicianose

Other name(s): vicianin hydrolase

Systematic name: (R)-vicianin β-D-glucohydrolase

Comments: Also hydrolyses, more slowly, (R)-amygdalin and (R)-prunasin, but not gentiobiose, linamarin or cellobiose.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 91608-93-4

References:

1. Kuroki, G., Lizotte, P.A. and Poulton, J.E. Catabolism of (R)-amygdalin and (R-viscianin by partially purified β-Glycosidases from Prunus serotina Ehrh and Davallia trichomanoides. Z. Natursforsch. C: Biosci. 39 (1984) 232-239.

[EC 3.2.1.119 created 1989]

EC 3.2.1.120

Accepted name: oligoxyloglucan β-glycosidase

Reaction: Hydrolysis of (1→4)-β-D-glucosidic links in oligoxyloglucans so as to remove successive isoprimeverose [i.e. α-xylo-(1→6)-β-D-glucosyl-] residues from the non-reducing chain ends

Other name(s): isoprimeverose-producing oligoxyloglucan hydrolase; oligoxyloglucan hydrolase

Systematic name: oligoxyloglucan xyloglucohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 97162-80-6

References:

1. Kato, Y., Matsushita, J., Kubodera, T. and Matsuda, K. A novel enzyme producing isoprimeverose from oligoxyloglucans of Aspergillus oryzae. J. Biochem. (Tokyo) 97 (1985) 801-810. [PMID: 4019436]

[EC 3.2.1.120 created 1989]

EC 3.2.1.121

Accepted name: polymannuronate hydrolase

Reaction: Endohydrolysis of the D-mannuronide linkages of polymannuronate

Other name(s): polymannuronic acid polymerase

Systematic name: poly(mannuronide) mannuronohydrolase

Comments: Does not act on alginic acid, which is a copolymer of polymannuronate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 99283-64-4

References:

1. Dunne, W.M., Jr. and Buckmire, F.L.A. Partial purification and characterization of a polymannuronic acid depolymerase produced by a mucoid strain of Pseudomonas aeruginosa isolated from a patient with cystic fibrosis. Appl. Environ. Microbiol. 50 (1985) 562-567. [PMID: 3935048]

[EC 3.2.1.121 created 1989]

EC 3.2.1.122

Accepted name: maltose-6'-phosphate glucosidase

Reaction: α-maltose 6′-phosphate + H2O = D-glucose + D-glucose 6-phosphate

Other name(s): phospho-α-glucosidase; maltose-6'-phosphate 6-phosphoglucohydrolase

Systematic name: α-maltose-6'-phosphate 6-phosphoglucohydrolase

Comments: Hydrolyses a variety of 6-phospho-α-D-glucosides, including α-maltose 6'-phosphate, α,α-trehalose 6-phosphate, sucrose 6-phosphate and p-nitrophenyl-α-D-glucopyranoside 6-phosphate (as a chromogenic substrate). The enzyme is activated by FeII, MnII, CoII and NiII. It is rapidly inactivated in air.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 98445-08-0

References:

1. Thompson, J., Gentry-Weeks, C.R., Nguyen, N.Y., Folk, J.E., Robrish, S.A. Purification from Fusobacterium mortiferum ATCC 25557 of a 6-phosphoryl-O-α-D-glucopyranosyl:6-phosphoglucohydrolase that hydrolyses maltose 6-phosphate and related phospho-α-D-glucosides. J. Bacteriol. 177 (1995) 2505-2512. [PMID: 7730284]

[EC 3.2.1.122 created 1989, modified 1999]

EC 3.2.1.123

Accepted name: endoglycosylceramidase

Reaction: oligoglycosylglucosyl-(1↔1)-ceramide + H2O = ceramide + oligoglycosylglucose

Other name(s): endoglycoceramidase; EGCase; glycosyl-N-acetyl-sphingosine 1,1-β-D-glucanohydrolase, oligoglycosylglucosylceramide glycohydrolase; oligoglycosylglucosyl(1↔1)ceramide glycohydrolase

Systematic name: oligoglycosylglucosyl-(1↔1)-ceramide glycohydrolase

Comments: An enzyme from Rhodococcus sp. that degrades various acidic and neutral glycosphingolipids to oligosaccharides and ceramides, by cleaving a glucosyl bond. Does not act on monoglycosylceramides. cf. EC 3.2.1.62 glycosylceramidase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 105503-61-5

References:

1. Ito, M. and Yamagata, T. A novel glycosphingolipid-degrading enzyme cleaves the linkage between the oligosaccharide and ceramide of neutral and acidic glycosphingolipids. J. Biol. Chem. 261 (1986) 14278-14282. [PMID: 3771534]

[EC 3.2.1.123 created 1989]

EC 3.2.1.124

Accepted name: 3-deoxy-2-octulosonidase

Reaction: Endohydrolysis of the β-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonate in capsular polysaccharides

Other name(s): 2-keto-3-deoxyoctonate hydrolase; octulosylono hydrolase; octulofuranosylono hydrolase; octulopyranosylonohydrolase

Systematic name: capsular-polysaccharide 3-deoxy-D-manno-2-octulosonohydrolase

Comments: The enzyme from a bacteriophage catalyses the depolymerization of capsular polysaccharides containing 3-deoxy-2-octulosonide in the cell wall of Escherichia coli.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 103171-48-8

References:

1. Altmann, F., Kwiatkowski, B., Stirm, S., März, L. and Unger, F.M. A bacteriophage-associated glycanase cleaving β-pyranosidic linkages of 3-deoxy-D-manno-2-octulosonic acid (KDO). Biochem. Biophys. Res. Commun. 136 (1986) 329-335. [PMID: 3707579]

[EC 3.2.1.124 created 1989]

EC 3.2.1.125

Accepted name: raucaffricine β-glucosidase

Reaction: raucaffricine + H2O = D-glucose + vomilenine

For diagram click here.

Other name(s): raucaffricine β-D-glucosidase; raucaffricine glucosidase

Systematic name: raucaffricine β-D-glucohydrolase

Comments: Highly specific; some other ajmalan glucoside alkaloids are hydrolysed, but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 102925-37-1

References:

1. Schübel, H., Stöckigt, J., Feicht, R. and Simon, H. Partial-purification and characterization of raucaffricine β-D-glucosidase from plant cell-suspension cultures of Rauwolfia serpentina benth. Helv. Chim. Acta 69 (1986) 538-547.

[EC 3.2.1.125 created 1989]

EC 3.2.1.126

Accepted name: coniferin β-glucosidase

Reaction: coniferin + H2O = D-glucose + coniferol

Other name(s): coniferin-hydrolyzing β-glucosidase

Systematic name: coniferin β-D-glucosidase

Comments: Also hydrolyses syringin, 4-cinnamyl alcohol β-glucoside and, more slowly, some other aryl β-glycosides. A plant cell-wall enzyme involved in the biosynthesis of lignin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 83869-30-1

References:

1. Hösel, W., Surholt, E. and Borgmann, E. Characterization of β-glucosidase isoenzymes possibly involved in lignification from chick pea (Cicer arietinum L.) cell suspension cultures. Eur. J. Biochem. 84 (1978) 487-492. [PMID: 25181]

2. Marcinowski, S. and Grisebach, H. Enzymology of lignification. Cell-wall bound β-glucosidase for coniferin from spruce (Picea abies) seedlings. Eur. J. Biochem. 87 (1978) 37-44. [PMID: 27355]

[EC 3.2.1.126 created 1989]

EC 3.2.1.127

Accepted name: 1,6-α-L-fucosidase

Reaction: Hydrolysis of (1→6)-linkages between α-L-fucose and N-acetyl-D-glucosamine in glycopeptides such as immunoglobulin G glycopeptide and fucosyl-asialo-agalacto-fetuin

Other name(s): α-L-fucosidase; 1,6-L-fucosyl-N-acetyl-D-glucosaminylglycopeptide fucohydrolase

Systematic name: 6-L-fucosyl-N-acetyl-D-glucosaminylglycopeptide fucohydrolase

Comments: The enzyme from Aspergillus niger does not act on 1,2-, 1,3-, or 1,4-L-fucosyl linkages.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 102925-35-9

References:

1. Yazawa, S., Madiyalakan, R., Chawda, R.P. and Matta, K.L. α-L-Fucosidase from Aspergillus niger: demonstration of a novel α-L-(1→6)-fucosidase acting on glycopeptides. Biochem. Biophys. Res. Commun. 136 (1986) 563-569. [PMID: 2423086]

[EC 3.2.1.127 created 1989]

EC 3.2.1.128

Accepted name: glycyrrhizinate β-glucuronidase

Reaction: glycyrrhizinate + H2O = (1→2)-β-D-glucuronosyl-D-glucuronate + glycyrrhetinate

Other name(s): glycyrrhizin β-hydrolase; glycyrrhizin hydrolase; glycyrrhizinic acid hydrolase

Systematic name: glycyrrhizinate glucuronosylhydrolase

Comments: The enzyme from Aspergillus niger is specific for the hydrolysis of the triterpenoid glycoside glycyrrhizinate from roots of Glycyrrhiza sp.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 102484-56-0

References:

1. Muro, T., Kuramoto, T., Imoto, K. and Okada, S. Purification and some properties of glycyrrhizinic acid hydrolase from Aspergillus niger GRM3. Agric. Biol. Chem. 50 (1986) 687-692.

[EC 3.2.1.128 created 1989]

EC 3.2.1.129

Accepted name: endo-α-sialidase

Reaction: Endohydrolysis of (2→8)-α-sialosyl linkages in oligo- or poly(sialic) acids

Other name(s): endo-N-acylneuraminidase; endoneuraminidase; endo-N-acetylneuraminidase; poly(α-2,8-sialosyl) endo-N-acetylneuraminidase; poly(α-2,8-sialoside) α-2,8-sialosylhydrolase; endosialidase; endo-N

Systematic name: polysialoside 2,8-α-sialosylhydrolase

Comments: Although the name endo-N-acetylneuraminidase has also been used for this enzyme, this is misleading since its activity is not restricted to acetylated substrates. An exo-α-sialidase activity is listed as EC 3.2.1.18 exo-α-sialidase. See also EC 4.2.2.15 anhydrosialidase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 91195-87-8

References:

1. Finne, J., Mäkelä, P.H. Cleavage of the polysialosyl units of brain glycoproteins by a bacteriophage endosialidase. Involvement of a long oligosaccharide segment in molecular interactions of polysialic acid. J. Biol. Chem. 260 (1985) 1265-1270. [PMID: 3968060]

2. Hallenbeck, P.C., Vimr, E.R., Yu, F., Bassler, B. and Troy, F.A. Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-α-2,8-sialosyl carbohydrate units. J. Biol. Chem. 262 (1987) 3553-3561. [PMID: 3546309]

3. Kitakima, K., Inoue, S., Inoue, Y. and Troy, F.A. Use of a bacteriophage-derived endo-N-acetylneuraminidase and an equine antipolysialyl antibody to characterize the polysialyl residues in salmonid fish egg polysialoglycoproteins. Substrate and immunospecificity studies. J. Biol. Chem. 263 (1988) 18269-18276. [PMID: 3142874]

4. Kwiatkowski, B., Boscheck, B., Thicle, H. and Stirm, S. Endo-N-acetylneuraminidase associated with bacteriophage particles. J. Virol. 43 (1982) 697-704. [PMID: 7109038]

5. Pelkonen, S., Pelkonen, J. and Finne, J. Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins. J. Virol. 65 (1989) 4409-4416. [PMID: 2778882]

6. Tombinson, S. and Taylor, P.W. Neuraminidase associated with coliphage E that specifically depolymerizes the Escherichia coli K1 capsular polysaccharide. J. Virol. 55 (1985) 374-378. [PMID: 3894684]

7. Cabezas, J.A. Some questions and suggestions on the type references of the official nomenclature (IUB) for sialidase(s) and endosialidase. Biochem. J. 278 (1991) 311-312. [PMID: 1883340]

[EC 3.2.1.129 created 1990, modified 1999]

EC 3.2.1.130

Accepted name: glycoprotein endo-α-1,2-mannosidase

Reaction: GlcMan9GlcNAc2-[protein] + H2O = Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) + α-D-glucosyl-(1→3)-α-D-mannopyranose

Glossary: GlcMan9GlcNAc2-[protein] = {α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc}-N-Asn-[protein]
Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) = {α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc}-N-Asn-[protein]

Other name(s): glucosylmannosidase; endo-α-D-mannosidase; endo-α-mannosidase; endomannosidase; glucosyl mannosidase; MANEA (gene name); glycoprotein glucosylmannohydrolase

Systematic name: glycoprotein glucosylmannohydrolase (configuration-retaining)

Comments: The enzyme catalyses the hydrolysis of the terminal α-D-glucosyl-(1→3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of N-glucosylated proteins during their processing in the Golgi apparatus. The name for the isomer is based on a nomenclature proposed by Prien et al [7].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 108022-16-8

References:

1. Lubas, W.A. and Spiro, R.G. Golgi endo-α-D-mannosidase from rat liver, a novel N-linked carbohydrate unit processing enzyme. J. Biol. Chem. 262 (1987) 3775-3781. [PMID: 3818665]

2. Tulsiani, D.R.P., Coleman, V.P. and Touster, O. Asparagine-linked glycoprotein biosynthesis in rat brain: identification of glucosidase I, glucosidase II, and endomannosidase (glucosyl mannosidase). Arch. Biochem. Biophys. 277 (1990) 114-121. [PMID: 2407194]

3. Hiraizumi, S., Spohr, U. and Spiro, R.G. Ligand affinity chromatographic purification of rat liver Golgi endomannosidase. J. Biol. Chem. 269 (1994) 4697-4700. [PMID: 8106437]

4. Spiro, M.J., Bhoyroo, V.D. and Spiro, R.G. Molecular cloning and expression of rat liver endo-α-mannosidase, an N-linked oligosaccharide processing enzyme. J. Biol. Chem. 272 (1997) 29356-29363. [PMID: 9361017]

5. Hamilton, S.R., Li, H., Wischnewski, H., Prasad, A., Kerley-Hamilton, J.S., Mitchell, T., Walling, A.J., Davidson, R.C., Wildt, S. and Gerngross, T.U. Intact α-1,2-endomannosidase is a typical type II membrane protein. Glycobiology 15 (2005) 615-624. [PMID: 15677381]

6. Hardt, B., Volker, C., Mundt, S., Salska-Navarro, M., Hauptmann, M. and Bause, E. Human endo-α1,2-mannosidase is a Golgi-resident type II membrane protein. Biochimie 87 (2005) 169-179. [PMID: 15760709]

7. Prien, J.M., Ashline, D.J., Lapadula, A.J., Zhang, H. and Reinhold, V.N. The high mannose glycans from bovine ribonuclease B isomer characterization by ion trap MS. J Am Soc Mass Spectrom 20 (2009) 539-556. [PMID: 19181540]

[EC 3.2.1.130 created 1990, modified 2017]

EC 3.2.1.131

Accepted name: xylan α-1,2-glucuronosidase

Reaction: Hydrolysis of (1→2)-α-D-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans

Other name(s): 1,2-α-glucuronidase; α-(1→2)-glucuronidase; xylan α-D-1,2-(4-O-methyl)glucuronohydrolase

Systematic name: xylan 2-α-D-(4-O-methyl)glucuronohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 114921-73-2

References:

1. Ishihara, M. and Shimizu, K. α-(1→2)-Glucuronidase in the enzymatic saccharification of hardwood xylan .1. Screening of α-glucuronidase producing fungi. Mokuzai Gakkaishi 34 (1988) 58-64.

[EC 3.2.1.131 created 1990]

EC 3.2.1.132

Accepted name: chitosanase

Reaction: Endohydrolysis of β-(1→4)-linkages between D-glucosamine residues in a partly acetylated chitosan

Systematic name: chitosan N-acetylglucosaminohydrolase

Comments: A whole spectrum of chitosanases are now known (for more details, see http://rbrzezinski.recherche.usherbrooke.ca/). They can hydrolyse various types of links in chitosan. The only constant property is the endohydrolysis of GlcN-GlcN links, which is common to all known chitosanases. One known chitosanase is limited to this link recognition [4], while the majority can also recognize GlcN-GlcNAc links or GlcNAc-GlcN links but not both. They also do not recognize GlcNAc-GlcNAc links in partly acetylated chitosan.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 51570-20-8

References:

1. Fenton, D.M. and Eveleigh, D.E. Purification and mode of action of a chitosanase from Penicillium islandicum. J. Gen. Microbiol. 126 (1981) 151-165.

2. Saito, J.-I., Kita, A., Higuchi, Y., Nagata, Y., Ando, A. and Miki, K. Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-Å resolution and its substrate recognition mechanism. J. Biol. Chem. 274 (1999) 30818-30825. [PMID: 10521473]

3. Izume, M., Nagae, S., Kawagishi, H., Mitsutomi, M. and Ohtakara, A. Action pattern of Bacillus sp. No. 7-M chitosanase on partially N-acetylated chitosan. Biosci. Biotechnol. Biochem. 56 (1992) 448-453. [PMID: 1368330]

4. Marcotte, E.M., Monzingo, A.F., Ernst, S.R., Brzezinski, R. and Robertus, J.D. X-ray structure of an anti-fungal chitosanase from Streptomyces N174. Nat. Struct. Biol. 3 (1996) 155-162. [PMID: 8564542]

[EC 3.2.1.132 created 1990, modified 2004]

EC 3.2.1.133

Accepted name: glucan 1,4-α-maltohydrolase

Reaction: hydrolysis of (1→4)-α-D-glucosidic linkages in polysaccharides so as to remove successive α-maltose residues from the non-reducing ends of the chains

Other name(s): maltogenic α-amylase; 1,4-α-D-glucan α-maltohydrolase

Systematic name: 4-α-D-glucan α-maltohydrolase

Comments: Acts on starch and related polysaccharides and oligosaccharides. The product is α-maltose; cf. EC 3.2.1.2 β-amylase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 160611-47-2

References:

1. Diderichsen, B. and Christiansen, L. Cloning of a maltogenic alpha-amylase from Bacillus stearothermophilus. FEMS Microbiol. Lett. 56 (1988) 53-59.

2. Outtrup, H. and Norman, B.E. Properties and application of a thermostable maltogenic amylase produced by a strain of Bacillus modified by recombinant-DNA techniques. Stärke 36 (1984) 405-411.

[EC 3.2.1.133 created 1992, modified 1999]

EC 3.2.1.134

Accepted name: difructose-anhydride synthase

Reaction: bis-D-fructose 2',1:2,1'-dianhydride + H2O = inulobiose

Other name(s): inulobiose hydrolase

Systematic name: bis-D-fructose 2',1:2,1'-dianhydride fructohydrolase

Comments: Produces difructose anhydride by the reverse reaction of partial hydrolysis, forming an α-fructosidic linkage.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 121479-55-8

References:

1. Matsuyama, T. and Tanaka, K. On the enzyme of Aspergillus fumigatus producing difructose anhydride I from inulobiose. Agric. Biol. Chem. 53 (1989) 831-832.

2. Matsuyama, T., Tanaka, K., Mashiko, M. and Kanamoto, M. Enzymic formation of di-D-fructose 1,2'; 2,1' dianhydride from inulobiose by Aspergillus fumigatus. J. Biochem. (Tokyo) 92 (1982) 1325-1328. [PMID: 6757245]

[EC 3.2.1.134 created 1992]

EC 3.2.1.135

Accepted name: neopullulanase

Reaction: Hydrolysis of pullulan to panose (6-α-D-glucosylmaltose)

Glossary: pullulan = a linear polymer of (1→6)-linked maltotriose units

Other name(s): pullulanase II

Systematic name: pullulan 4-D-glucanohydrolase (panose-forming)

Comments: cf. EC 3.2.1.41 (pullulanase ) and EC 3.2.1.57 (isopullulanase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 119632-58-5

References:

1. Imanaka, T. and Kuriki, T. Pattern of action of Bacillus stearothermophilus neopullulanase on pullulan. J. Bacteriol. 171 (1989) 369-374. [PMID: 2914851]

[EC 3.2.1.135 created 1992]

EC 3.2.1.136

Accepted name: glucuronoarabinoxylan endo-1,4-β-xylanase

Reaction: Endohydrolysis of (1→4)-β-D-xylosyl links in some glucuronoarabinoxylans

Other name(s): feraxan endoxylanase; feraxanase; endoarabinoxylanase; glucuronoxylan xylohydrolase; glucuronoxylanase; glucuronoxylan xylanohydrolase; glucuronoarabinoxylan 1,4-β-D-xylanohydrolase

Systematic name: glucuronoarabinoxylan 4-β-D-xylanohydrolase

Comments: High activity towards feruloylated arabinoxylans from cereal plant cell walls.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 123609-77-8

References:

1. Nishitani, K. and Nevins, D.J. Enzymic analysis of feruloylated arabinoxylans (Feraxan) derived from Zea mays cell walls. I. Purification of novel enzymes capable of dissociating Feraxan fragments from Zea mays coleoptile cell wall. Plant Physiol. 87 (1988) 883-890.

[EC 3.2.1.136 created 1992]

EC 3.2.1.137

Accepted name: mannan exo-1,2-1,6-α-mannosidase

Reaction: Hydrolysis of (1→2)-α-D- and (1→6)-α-D- linkages in yeast mannan, releasing D-mannose

Other name(s): exo-1,2-1,6-α-mannosidase

Systematic name: (1→2)-(1→6)-α-D-mannan D-mannohydrolase

Comments: Mannose residues linked α-D-1,3- are also released, but very slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 123175-72-4

References:

1. Takegawa, K., Miki, S., Jikibara, T. and Iwahara, S. Purification and characterization of exo-α-D-mannosidase from a Cellulomonas sp. Biochim. Biophys. Acta 991 (1989) 431-437.

[EC 3.2.1.137 created 1992]

[EC 3.2.1.138 Transferred entry: now EC 4.2.2.15 anhydrosialidase. (EC 3.2.1.138 created 1992, deleted 2003)]

EC 3.2.1.139

Accepted name: α-glucuronidase

Reaction: an α-D-glucuronoside + H2O = an alcohol + D-glucuronate

Other name(s): α-glucosiduronase

Systematic name: α-D-glucosiduronate glucuronohydrolase

Comments: considerable differences in the specificities of the enzymes from different fungi for α-D-glucosiduronates have been reported. Activity is also found in the snail.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37259-81-7

References:

1. Puls, J. α-Glucuronidases in the hydrolysis of wood xylans. In Xylans and Xylanases (J. Visser et al., Eds.), Elsevier, Amsterdam, (1992) pp. 213-224.

2. Uchida, H., Nanri, T., Kawabata, Y., Kusakabe, I., Murakami, K. Purification and characterization of intracellular α-glucuronidase from Aspergillus niger. Biosci. Biotechnol. Biochem. 56 (1992) 1608-1615.

[EC 3.2.1.139 created 1999]

EC 3.2.1.140

Accepted name: lacto-N-biosidase

Reaction: β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-D-Glc + H2O = β-D-Gal-(1→3)-D-GlcNAc + β-D-Gal-(1→4)-D-Glc

Glossary: β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-D-Glc = lacto-N-tetraose
β-D-Gal-(1→3)-D-GlcNAc = lacto-N-biose
β-D-Gal-(1→4)-D-Glc = lactose

Systematic name: oligosaccharide lacto-N-biosylhydrolase

Comments: The enzyme from Streptomyces specifically hydrolyses the terminal lacto-N-biosyl residue (β-D-Gal-(1→3)-D-GlcNAc) from the non-reducing end of oligosaccharides with the structure β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→R). Lacto-N-hexaose (β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-D-Glc) is hydrolysed to form first lacto-N-tetraose plus lacto-N-biose, with the subsequent formation of lactose. Oligosaccharides in which the non-reducing terminal Gal or the penultimate GlcNAc are replaced by fucose or sialic acid are not substrates. Asialo GM1 tetraose (β-D-Gal-(1→3)-β-D-GalNAc-(1→3)-β-D-Gal-(1→4)-D-Glc) is hydrolysed very slowly, but lacto-N-neotetraose (β-D-Gal-(1→4)-β-D-GalNAc-(1→3)-β-D-Gal-(1→4)-D-Glc) is not a substrate

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 146359-52-6

References:

1. Sano, M., Hayakawa, K., Kato, I. An enzyme releasing lacto-N-biose from oligosaccharides. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 8512-8516. [PMID: 1528855]

2. Sano, M., Hayakawa, K., Kato, I. Purification and characterization of an enzyme releasing lacto-N-biose from oligosaccharides with type 1 chain. J. Biol. Chem. 268 (1993) 18560-18566. [PMID: 7689556]

[EC 3.2.1.140 created 1999]

EC 3.2.1.141

Accepted name: 4-α-D-{(1→4)-α-D-glucano}trehalose trehalohydrolase

Reaction: hydrolysis of (1→4)-α-D-glucosidic linkage in 4-α-D-[(1→4)-α-D-glucanosyl]n trehalose to yield trehalose and (1→4)-α-D-glucan

Other name(s): malto-oligosyltrehalose trehalohydrolase

Systematic name: 4-α-D-(1,4-α-D-glucano)trehalose glucanohydrolase (trehalose-producing)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 170780-50-4

References:

1. Maruta, K., Nakada, T., Kubota, M., Chaen, H., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. Formation of trehalose from maltooligosaccharides by a novel enzymatic system. Biosci. Biotechnol. Biochem. 59 (1995) 1829-1834. [PMID: 8534970]

2. Nakada, T., Maruta, K., Mitsuzumi, H., Kubota, M., Chaen, H., Sugimoto, T., Kurimoto M., Tsujisaka, Y. Purification and characterization of a novel enzyme, maltooligosyl trehalose trehalohydrolase, from Arthrobacter sp. Q36. Biosci. Biotechnol. Biochem. 59 (1995) 2215-2218. [PMID: 8611745]

3. Nakada, T., Ikegami, S., Chaen, H., Kubota, M., Fukuda, S., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. Purification and characterization of thermostable maltooligosyl trehalose trehalohydrolase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biosci. Biotechnol. Biochem. 60 (1996) 267-270. [PMID: 9063974]

[EC 3.2.1.141 created 1999]

EC 3.2.1.142

Accepted name: limit dextrinase

Reaction: Hydrolysis of (1→6)-α-D-glucosidic linkages in α- and β-limit dextrins of amylopectin and glycogen, and in amylopectin and pullulan

Glossary: pullulan = a linear polymer of (1→6)-linked maltotriose units

Other name(s): R-enzyme; amylopectin-1,6-glucosidase; dextrin α-1,6-glucanohydrolase

Systematic name: dextrin 6-α-glucanohydrolase

Comments: Plant enzymes with little or no action on glycogen. Action on amylopectin is incomplete, but action on α-limit dextrins is complete. Maltose is the smallest sugar it can release from an α-(1<→6)-linkage.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Gordon, R.W., Manners, D.J. and Stark, J.R. The limit dextrinase of the broad bean (Vicia faba). Carbohydr. Res. 42 (1975) 125-134.

2. Manners, D.J. Observations on the specificity and nomenclature of starch debranching enzymes. J. Appl. Glycosci. 44 (1997) 83-85.

[EC 3.2.1.142 created 2000]

EC 3.2.1.143

Accepted name: poly(ADP-ribose) glycohydrolase

Reaction: hydrolyses poly(ADP-ribose) at glycosidic (1"-2') linkage of ribose-ribose bond to produce free ADP-D-ribose

For diagram click here.

Comments: Specific to (1"-2') linkage of ribose-ribose bond of poly(ADP-D-ribose).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9068-16-0

References:

1. Miwa, M. and Sugimura, T. Splitting of the ribose-ribose linkage of poly(adenosine diphosphate-ribose) by a calf thymus extract. J. Biol. Chem. 246 (1971) 6362-6364. [PMID: 4331388]

2. Lin, W., Ame, J.C., Aboul-Ela, N., Jacobson, E.L. and Jacobson, M.K. Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 272 (1997) 11895-11901. [PMID: 9115250]

[EC 3.2.1.143 created 2000]

EC 3.2.1.144

Accepted name: 3-deoxyoctulosonase

Reaction: 3-deoxyoctulosonyl-lipopolysaccharide + H2O = 3-deoxyoctulosonic acid + lipopolysaccharide

Other name(s): α-Kdo-ase

Systematic name: 3-deoxyoctulosonyl-lipopolysaccharide hydrolase

Comments: Releases Kdo (α- and β-linked 3-deoxy-D-manno-octulosonic acid) from different lipopolysaccharides, including Re-LPS from Escherichia coli and Salmonella, Rd-LPS from S. minnesota, and de-O-acyl-re-LPS. 4-Methylumbelliferyl-α-Kdo (α-Kdo-OMec) is also a substrate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 199128-67-1

References:

1. Li, Y.T., Wang, L.X., Pavlova, N.V., Li, S.C. and Lee, Y.C. α-KDOase activity in oyster and synthesis of α- and β-4-methylumbelliferyl ketosides of 3-deoxy-D-manno-octulosonic acid (KDO) J. Biol. Chem. 272 (1997) 26419-26424. [PMID: 9334217]

[EC 3.2.1.144 created 2000]

EC 3.2.1.145

Accepted name: galactan 1,3-β-galactosidase

Reaction: Hydrolysis of terminal, non-reducing β-D-galactose residues in (1→3)-β-D-galactopyranans

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, 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. [PMID: 7805066]

[EC 3.2.1.145 created 2001]

EC 3.2.1.146

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.

[EC 3.2.1.146 created 2001]

EC 3.2.1.147

Accepted name: thioglucosidase

Reaction: a thioglucoside + H2O = a sugar + a thiol

Other name(s): myrosinase; sinigrinase; sinigrase

Systematic name: thioglucoside glucohydrolase

Comments: Has a wide specificity for thioglycosides.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-38-1

References:

1. Goodman, I., Fouts, J.R., Bresnick, E., Menegas, R. and Hitchings, G.H. A mammalian thioglucosidase. Science 130 (1959) 450-451.

2. Pigman, W.W. Action of almond emulsin on the phenyl glucosides of synthetic sugars and on β-thiophenyl d-glucoside. J. Res. Nat. Bur. Stand. 26 (1941) 197-204.

[EC 3.2.1.147 created 1972 as EC 3.2.3.1, transferred 2001 to EC 3.2.1.147]

[EC 3.2.1.148 Deleted entry: ribosylhomocysteinase. The activity is most probably attributable to EC 4.4.1.21 S-ribosylhomocysteine lyase (EC 3.2.1.148 created 1972 as EC 3.3.1.3, transferred 2001 to EC 3.2.1.148, transferred 2004 to EC 3.13.1.2, deleted 2005)]

EC 3.2.1.149

Accepted name: β-primeverosidase

Reaction: a 6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside + H2O = 6-O-(β-D-xylopyranosyl)-β-D-glucopyranose + an alcohol

Glossary
primeverose = 6-O-(β-D-xylopyranosyl)-D-glucose
vicianose = 6-O-(α-L-arabinopyranosyl)-D-glucose

Systematic name: 6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside 6-O-(β-D-xylosyl)-β-D-glucohydrolase

Comments: The enzyme is responsible for the formation of the alcoholic aroma in oolong and black tea. In addition to β-primeverosides [i.e. 6-O-(β-D-xylopyranosyl)-β-D-glucopyranosides], it also hydrolyses 6-O-(β-D-apiofuranosyl)-β-D-glucopyranosides and, less rapidly, β-vicianosides and 6-O-(α-L-arabinofuranosyl)-β-D-glucopyranosides, but not β-glucosides. Geranyl-, linaloyl-, benzyl- and p-nitrophenol glycosides are all hydrolysed.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 884593-92-4

References

1. Ijima, Y., Ogawa, K., Watanabe, N., Usui, T., Ohnishi-Kameyama, M., Nagata, T. and Sakata, K. Characterization of β-primeverosidase, being concerned with alcoholic aroma formation in tea leaves to be processed into black tea, and preliminary observations on its substrate specificity. J. Agric. Food Chem. 46 (1998) 1712-1718.

2. Ogawa, K., Ijima, Y., Guo, W., Watanabe, N., Usui, T., Dong, S., Tong, Q. and Sakata, K. Purification of a β-primeverosidase concerned with alcoholic aroma formation in tea leaves (cv. Shuxian) to be processed to oolong tea. J. Agric. Food Chem. 45 (1997) 877-882.

[EC 3.2.1.149 created 2001]

EC 3.2.1.150

Accepted name: oligoxyloglucan reducing-end-specific cellobiohydrolase

Reaction: Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a (1→4)-β-linked glucan carrying α-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted.

Systematic name: oligoxyloglucan reducing-end cellobiohydrolase

Comments: The enzyme is found in the fungus Geotrichum sp. M128. The substrate is a hemicellulose found in plant cell walls.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 753502-07-7

References:

1. Yaoi, K. and Mitsuishi, Y. Purification, characterization, cloning, and expression of a novel xyloglucan-specific glycosidase, oligoxyloglucan reducing end-specific cellobiohydrolase. J. Biol. Chem. 277, (2002) 48276-48281. [PMID: 12374797]

[EC 3.2.1.150 created 2003]


Continued with EC 3.2.1.151 to EC 3.2.1.208
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