See the following file for:
EC 3.2.1.151 to EC 3.2.1.226
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, PDB, 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]
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, PDB, 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]
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]
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, PDB, 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.
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]
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, PDB, 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]
Accepted name: protein-glucosylgalactosylhydroxylysine glucosidase
Reaction: [collagen]-(5R)-5-O-[α-D-glucosyl-(1→2)-β-D-galactosyl]-5-hydroxy-L-lysine + H2O = D-glucose + [collagen]-(55R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine
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: The enzyme specifically hydrolyses glucose from α-D-glucosyl-(1→2)-β-D-galactosyl disaccharide units that are linked to hydroxylysine residues of collagen and collagen-like proteins. Acetylation of the ε-amino group of the glycosylated hydroxylysine abolishes activity.
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]
4. Hamazaki, H. and Hamazaki, M.H. Catalytic site of human protein-glucosylgalactosylhydroxylysine glucosidase: Three crucial carboxyl residues were determined by cloning and site-directed mutagenesis. Biochem. Biophys. Res. Commun. 469 (2016) 357–362. [PMID: 26682924]
Accepted name: lactase
Reaction: lactose + H2O = β-D-galactose + D-glucose
Glossary: lactose = β-D-galactopyranosyl-(1→4)-α-D-glucopyranose
Other name(s): lactase-phlorizin hydrolase; LPH (gene name); LCT (gene name)
Systematic name: lactose galactohydrolase (configuration-retaining)
Comments: The enzyme from intestinal mucosa contains two glycosyl hydrolase domains, both of which belong to glycosyl hydrolase family 1 (GH1). While the first domain catalyses the activity described here, the second domain 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. 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]
2. 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]
3. Lorenz-Meyer, H., Blum, A.L., Haemmerli, H.P. and Semenza, G. A second enzyme defect in acquired lactase deficiency: lack of small-intestinal phlorizin-hydrolase. Eur. J. Clin. Invest. 2 (1972) 326-331. [PMID: 5082068]
4. 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]
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. 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]
7. Zecca, L., Mesonero, J.E., Stutz, A., Poiree, J.C., Giudicelli, J., Cursio, R., Gloor, S.M. and Semenza, G. Intestinal lactase-phlorizin hydrolase (LPH): the two catalytic sites; the role of the pancreas in pro-LPH maturation. FEBS Lett. 435 (1998) 225-228. [PMID: 9762914]
8. Arribas, J.C., Herrero, A.G., Martin-Lomas, M., Canada, F.J., He, S. and Withers, S.G. Differential mechanism-based labeling and unequivocal activity assignment of the two active sites of intestinal lactase/phlorizin hydrolase. Eur. J. Biochem. 267 (2000) 6996-7005. [PMID: 11106409]
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 3.2.1.110 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)]
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, PDB, 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]
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]
Accepted name: mannosyl-oligosaccharide 1,2-α-mannosidase
Reaction: (1) Man9GlcNAc2-[protein] + 4 H2O = Man5GlcNAc2-[protein] + 4 β-D-mannopyranose (overall reaction)
(1a) Man9GlcNAc2-[protein] + H2O = Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) + β-D-mannopyranose
(1b) Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) + H2O = Man7GlcNAc2-[protein] (isomer 7A1,2,3B2) + β-D-mannopyranose
(1c) Man7GlcNAc2-[protein] (isomer 7A1,2,3B2) + H2O = Man6GlcNAc2-[protein] (isomer 6A1,2B2) + β-D-mannopyranose
(1d) Man6GlcNAc2-[protein] (isomer 6A1,2B2) + H2O = Man5GlcNAc2-[protein] + β-D-mannopyranose
(2) Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,3) + 3 H2O = Man5GlcNAc2-[protein] + 3 β-D-mannopyranose (overall reaction)
(2a) Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,3) + H2O = Man7GlcNAc2-[protein] (isomer 7A1,2,3B1) + β-D-mannopyranose
(2b) Man7GlcNAc2-[protein] (isomer 7A1,2,3B1) + H2O = Man6GlcNAc2-[protein] (isomer 6A1,2,3) + β-D-mannopyranose
(2c) Man6GlcNAc2-[protein] (isomer 6A1,2,3) + H2O = Man5GlcNAc2-[protein] + β-D-mannopyranose
Glossary: Man9GlcNAc2-[protein] = [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]
Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,3) = [α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Man5GlcNAc2-[protein] = [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]
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; MAN1A1 (gene name); MAN1A2 (gene name); MAN1C1 (gene name); 2-α-mannosyl-oligosaccharide α-D-mannohydrolase
Systematic name: Man9GlcNAc2-[protein] α-2-mannohydrolase (configuration-inverting)
Comments: This family of mammalian enzymes, located in the Golgi system, participates in the maturation process of N-glycans that leads to formation of hybrid and complex structures. The enzymes catalyse the hydrolysis of the four (1→2)-linked α-D-mannose residues from the Man9GlcNAc2 oligosaccharide attached to target proteins as described in reaction (1). Alternatively, the enzymes act on the Man8GlcNAc2 isomer formed by EC 3.2.1.209, endoplasmic reticulum Man9GlcNAc2 1,2-α-mannosidase, as described in reaction (2). The enzymes are type II membrane proteins, require Ca2+, and use an inverting mechanism. While all three human enzymes can catalyse the reactions listed here, some of the enzymes can additionally catalyse hydrolysis in an alternative order, generating additional isomeric intermediates, although the final product is the same. The names of the isomers listed here are based on a nomenclature system proposed by Prien et al. [7].
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]
3. Bieberich, E. and Bause, E. Man9-mannosidase from human kidney is expressed in COS cells as a Golgi-resident type II transmembrane N-glycoprotein. Eur. J. Biochem. 233 (1995) 644-649. [PMID: 7588811]
4. Tremblay, L.O., Campbell Dyke, N. and Herscovics, A. Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human α1,2-mannosidase gene involved in N-glycan maturation. Glycobiology 8 (1998) 585-595. [PMID: 9592125]
5. Lal, A., Pang, P., Kalelkar, S., Romero, P.A., Herscovics, A. and Moremen, K.W. Substrate specificities of recombinant murine Golgi α1,2-mannosidases IA and IB and comparison with endoplasmic reticulum and Golgi processing α1,2-mannosidases. Glycobiology 8 (1998) 981-995. [PMID: 9719679]
6. Tremblay, L.O. and Herscovics, A. Characterization of a cDNA encoding a novel human Golgi α 1, 2-mannosidase (IC) involved in N-glycan biosynthesis. J. Biol. Chem. 275 (2000) 31655-31660. [PMID: 10915796]
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]
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]
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 enzyme; 1,2-α-D-glucosyl-branched-dextran 2-glucohydrolase
Systematic name: (1→2)-α-D-glucosyl-branched-dextran 2-glucohydrolase
Comments: Has a much lower activity with kojibiose and kojitriose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72840-94-9
References:
1. Kobayashi, M., Mitsuishi, Y., and Matsuda, K. Pronounced hydrolysis of highly branched dextrans with a new type of dextranase. Biochem Biophys Res Commun 80(2) (1978) 306-312. [PMID: 623663]
2. 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.
3. 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]
4. Miyazaki, T., Tanaka, H., Nakamura, S., Dohra, H. and Funane, K. Identification and characterization of dextran α-1,2-debranching enzyme from Microbacterium dextranolyticum. Journal of Applied Glycoscience (2023) .
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.
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.
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.
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.
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]
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]
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]
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]
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]
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.
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]
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]
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.
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]
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, PDB, 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]
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, PDB, 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.
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]
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 3.2.1.134 Transferred entry: difructose-dianhydride-I hydrolase. Now EC 4.2.1.179, difructose-dianhydride-I hydro-lyase (EC 3.2.1.134 created 1992, deleted 2021)]
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]
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.
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 3.2.1.138 Transferred entry: now EC 4.2.2.15 anhydrosialidase. (EC 3.2.1.138 created 1992, deleted 2003)]
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.
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, PDB, 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]
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]
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.
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]
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]
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, 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. [PMID: 7805066]
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.
Accepted name: thioglucosidase
Reaction: a thioglucoside + H2O = a sugar + a thiol
For diagram click here.
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 3.2.1.148 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)]
Accepted name: β-primeverosidase
Reaction: a 6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside + H2O = 6-O-(β-D-xylopyranosyl)-β-D-glucopyranose + an alcohol
Glossary
primeverose = 6-O-(β-D-xylopyranosyl)-D-glucose
vicianose = 6-O-(α-L-arabinopyranosyl)-D-glucose
Systematic name: 6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside 6-O-(β-D-xylosyl)-β-D-glucohydrolase
Comments: The enzyme is responsible for the formation of the alcoholic aroma in oolong and black tea. In addition to β-primeverosides [i.e. 6-O-(β-D-xylopyranosyl)-β-D-glucopyranosides], it also hydrolyses 6-O-(β-D-apiofuranosyl)-β-D-glucopyranosides and, less rapidly, β-vicianosides and 6-O-(α-L-arabinofuranosyl)-β-D-glucopyranosides, but not β-glucosides. Geranyl-, linaloyl-, benzyl- and p-nitrophenol glycosides are all hydrolysed.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 884593-92-4
References
1. Ijima, Y., Ogawa, K., Watanabe, N., Usui, T., Ohnishi-Kameyama, M., Nagata, T. and Sakata, K. Characterization of β-primeverosidase, being concerned with alcoholic aroma formation in tea leaves to be processed into black tea, and preliminary observations on its substrate specificity. J. Agric. Food Chem. 46 (1998) 1712-1718.
2. Ogawa, K., Ijima, Y., Guo, W., Watanabe, N., Usui, T., Dong, S., Tong, Q. and Sakata, K. Purification of a β-primeverosidase concerned with alcoholic aroma formation in tea leaves (cv. Shuxian) to be processed to oolong tea. J. Agric. Food Chem. 45 (1997) 877-882.
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]