The Enzyme Database

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EC 3.2.1.51     
Accepted name: α-L-fucosidase
Reaction: an α-L-fucoside + H2O = L-fucose + an alcohol
Other name(s): α-fucosidase
Systematic name: α-L-fucoside fucohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9037-65-4
References:
1.  Levvy, G.A. and McAllan, A. Mammalian fucosidases. 2. α-L-Fucosidase. Biochem. J. 80 (1961) 435–439. [PMID: 13761578]
2.  Reglero, A. and Cabezas, J.A. Glycosidases of molluscs. Purification and properties of α-L-fucosidase from Chamelea gallina L. Eur. J. Biochem. 66 (1976) 379–387. [DOI] [PMID: 7458]
3.  Tanaka, K., Nakano, T., Noguchi, S. and Pigman, W. Purification of α-L-fucosidase of abalone livers. Arch. Biochem. Biophys. 126 (1968) 624–633. [DOI] [PMID: 5672520]
[EC 3.2.1.51 created 1972]
 
 
EC 3.2.1.52     
Accepted name: β-N-acetylhexosaminidase
Reaction: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-β-D-hexosaminides
Other name(s): hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-β-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhexosaminidase; β-N-acetyl-D-hexosaminidase; β-N-acetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase; β-D-hexosaminidase
Systematic name: β-N-acetyl-D-hexosaminide N-acetylhexosaminohydrolase
Comments: Acts on N-acetylglucosides and N-acetylgalactosides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-33-3
References:
1.  Cabezas, J.A. Some comments on the type references of the official nomenclature (IUB) for β-N-acetylglucosaminidase, β-N-acetylhexosaminidase and β-N-acetylgalactosaminidase. Biochem. J. 261 (1989) 1059–1060. [PMID: 2529847]
2.  Calvo, P., Reglero, A. and Cabezas, J.A. Purification and properties of β-N-acetylhexosaminidase from the mollusc Helicella ericetorum Muller. Biochem. J. 175 (1978) 743–750. [PMID: 33660]
3.  Frohwein, Y.S. and Gatt, S. Isolation of β-N-acetylhexosaminidase, β-N-acetylglucosaminidase, and β-N-acetylgalactosaminidase from calf brain. Biochemistry 6 (1967) 2775–2782. [PMID: 6055190]
4.  Li, S.-C. and Li, Y.-T. Studies on the glycosidases of jack bean meal. 3. Crystallization and properties of β-N-acetylhexosaminidase. J. Biol. Chem. 245 (1970) 5153–5160. [PMID: 5506280]
[EC 3.2.1.52 created 1972 (EC 3.2.1.30 created 1961, incorporated 1992 [EC 3.2.1.29 created 1961, incorporated 1972])]
 
 
EC 3.2.1.53     
Accepted name: β-N-acetylgalactosaminidase
Reaction: Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-β-D-galactosaminides
Other name(s): N-acetyl-β-galactosaminidase; N-acetyl-β-D-galactosaminidase; β-acetylgalactosaminidase; β-D-N-acetylgalactosaminidase; N-acetylgalactosaminidase
Systematic name: β-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-43-7
References:
1.  Frohwein, Y.S. and Gatt, S. Isolation of β-N-acetylhexosaminidase, β-N-acetylglucosaminidase, and β-N-acetylgalactosaminidase from calf brain. Biochemistry 6 (1967) 2775–2782. [PMID: 6055190]
2.  Hoogwinkel, G.J.M., Veltkamp, W.A., Overdijk, B. and Lisman, J.W. Electrophoretic separation of β-N-acetylhexosaminidases of human and bovine brain and liver and of Tay-Sachs brain tissue. Hoppe-Seylers Z. Physiol. Chem. 353 (1972) 839–841. [PMID: 5069351]
[EC 3.2.1.53 created 1972]
 
 
EC 3.2.1.54     
Accepted name: cyclomaltodextrinase
Reaction: cyclomaltodextrin + H2O = linear maltodextrin
Other name(s): cycloheptaglucanase; cyclohexaglucanase; cyclodextrinase; cyclomaltodextrin dextrin-hydrolase (decyclizing)
Systematic name: cyclomaltodextrin dextrin-hydrolase (ring-opening)
Comments: Also hydrolyses linear maltodextrin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-41-8
References:
1.  DePinto, J.A. and Campbell, L.L. Purification and properties of the cyclodextrinase of Bacillus macerans. Biochemistry 7 (1968) 121–125. [PMID: 4922856]
[EC 3.2.1.54 created 1972 (EC 3.2.1.12 and EC 3.2.1.13 both created 1961 and incorporated 1976)]
 
 
EC 3.2.1.55     
Accepted name: non-reducing end α-L-arabinofuranosidase
Reaction: Hydrolysis of terminal non-reducing α-L-arabinofuranoside residues in α-L-arabinosides.
Other name(s): arabinosidase (ambiguous); α-arabinosidase; α-L-arabinosidase; α-arabinofuranosidase; polysaccharide α-L-arabinofuranosidase; α-L-arabinofuranoside hydrolase; L-arabinosidase (ambiguous); α-L-arabinanase
Systematic name: α-L-arabinofuranoside non-reducing end α-L-arabinofuranosidase
Comments: The enzyme acts on α-L-arabinofuranosides, α-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Some β-galactosidases (EC 3.2.1.23) and β-D-fucosidases (EC 3.2.1.38) also hydrolyse α-L-arabinosides. cf. EC 3.2.1.185, non-reducing end β-L-arabinofuranosidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-74-7
References:
1.  Tagawa, K. and Kaji, A. Preparation of L-arabinose-containing polysaccharides and the action of an α-L-arabinofuranosidase on these polysaccharides. Carbohydr. Res. 11 (1969) 293–301.
2.  Kaji, A. and Tagawa, K. Purification, crystallization and amino acid composition of α-L-arabinofuranosidase from Aspergillus niger. Biochim. Biophys. Acta 207 (1970) 456–464. [DOI] [PMID: 5452669]
3.  Kaji, A. and Yoshihara, O. Properties of purified α-L-arabinofuranosidase from Corticium rolfsii. Biochim. Biophys. Acta 250 (1971) 367–371. [DOI] [PMID: 5143344]
4.  Margolles-Clark, E., Tenkanen, M., Nakari-Setala, T. and Penttila, M. Cloning of genes encoding α-L-arabinofuranosidase and β-xylosidase from Trichoderma reesei by expression in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 62 (1996) 3840–3846. [PMID: 8837440]
5.  Inacio, J.M., Correia, I.L. and de Sa-Nogueira, I. Two distinct arabinofuranosidases contribute to arabino-oligosaccharide degradation in Bacillus subtilis. Microbiology 154 (2008) 2719–2729. [DOI] [PMID: 18757805]
[EC 3.2.1.55 created 1972, modified 1976 (EC 3.2.1.79 created 1972, incorporated 1976), modified 2013]
 
 
EC 3.2.1.56     
Accepted name: glucuronosyl-disulfoglucosamine glucuronidase
Reaction: 3-D-glucuronosyl-N2,6-disulfo-β-D-glucosamine + H2O = D-glucuronate + N2,6-disulfo-D-glucosamine
Other name(s): glycuronidase; 3-D-glucuronsyl-2-N,6-disulfo-β-D-glucosamine glucuronohydrolase
Systematic name: 3-D-glucuronsyl-N2,6-disulfo-β-D-glucosamine glucuronohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-42-9
References:
1.  Dietrich, C.P. Enzymic degradation of heparin. A glucosaminidase and a glycuronidase from Flavobacterium heparinum. Biochemistry 8 (1969) 2089–2094. [PMID: 5785227]
[EC 3.2.1.56 created 1972]
 
 
EC 3.2.1.57     
Accepted name: isopullulanase
Reaction: Hydrolysis of pullulan to isopanose (6-α-maltosylglucose)
Glossary: pullulan = a linear polymer of (1→6)-linked maltotriose units
Systematic name: pullulan 4-glucanohydrolase (isopanose-forming)
Comments: The enzyme has practically no action on starch. Panose (4-α-isomaltosylglucose) is hydrolysed to isomaltose and glucose. cf. EC 3.2.1.41 (pullulanase) and EC 3.2.1.135 (neopullulanase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-43-0
References:
1.  Sakano, Y., Masuda, N. and Kobayashi, T. Hydrolysis of pullulan by a novel enzyme from Aspergillus niger. Agric. Biol. Chem. 35 (1971) 971–973.
[EC 3.2.1.57 created 1972]
 
 
EC 3.2.1.58     
Accepted name: glucan 1,3-β-glucosidase
Reaction: Successive hydrolysis of β-D-glucose units from the non-reducing ends of (1→3)-β-D-glucans, releasing α-glucose
Other name(s): exo-1,3-β-glucosidase; β-1,3-glucan exo-hydrolase; exo (1→3)-glucanohydrolase; 1,3-β-glucan glucohydrolase
Systematic name: 3-β-D-glucan glucohydrolase
Comments: Acts on oligosaccharides, but very slowly on laminaribiose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9073-49-8
References:
1.  Barras, D.R. and Stone, B.A. β-1,3-Glucan hydrolases from Euglena gracilis. I. The nature of the hydrolases. Biochim. Biophys. Acta 191 (1969) 329–341. [DOI] [PMID: 5354264]
2.  Barras, D.R. and Stone, B.A. β-1,3-Glucan hydrolases from Euglena gracilis. II. Purification and properties of the β-1,3-glucan exo-hydrolase. Biochim. Biophys. Acta 191 (1969) 342–353. [DOI] [PMID: 5354265]
[EC 3.2.1.58 created 1972]
 
 
EC 3.2.1.59     
Accepted name: glucan endo-1,3-α-glucosidase
Reaction: Endohydrolysis of (1→3)-α-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran
Other name(s): endo-1,3-α-glucanase; mutanase; endo-(1→3)-α-glucanase; cariogenase; cariogenanase; endo-1,3-α-D-glucanase; 1,3(1,3;1,4)-α-D-glucan 3-glucanohydrolase
Systematic name: 3-α-D-glucan 3-glucanohydrolase
Comments: Products from pseudonigeran (1,3-α-D-glucan) are nigerose and α-D-glucose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-84-7
References:
1.  Hasegawa, S., Nordin, J.H. and Kirkwood, S. Enzymes that hydrolyze fungal cell wall polysaccharides. I. Purification and properties of an endo-α-D-(1-3)-glucanase from Trichoderma. J. Biol. Chem. 244 (1969) 5460–5470. [PMID: 5388595]
[EC 3.2.1.59 created 1972]
 
 
EC 3.2.1.60     
Accepted name: glucan 1,4-α-maltotetraohydrolase
Reaction: Hydrolysis of (1→4)-α-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends
Other name(s): exo-maltotetraohydrolase; 1,4-α-D-glucan maltotetraohydrolase
Systematic name: 4-α-D-glucan maltotetraohydrolase
Comments: Compare EC 3.2.1.2 β-amylase, which removes successive maltose residues, and EC 3.2.1.98 (glucan 1,4-α-maltohexaosidase) and EC 3.2.1.116 (glucan 1,4-α-maltotriohydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-44-1
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.
2.  Robyt, J.F. and Ackerman, R.J. Isolation, purification, and characterization of a maltotetraose-producing amylase from Pseudomonas stutzeri. Arch. Biochem. Biophys. 145 (1971) 105–114. [DOI] [PMID: 5123132]
[EC 3.2.1.60 created 1972]
 
 
EC 3.2.1.61     
Accepted name: mycodextranase
Reaction: Endohydrolysis of (1→4)-α-D-glucosidic linkages in α-D-glucans containing both (1→3)- and (1→4)-bonds
Other name(s): 1,3-1,4-α-D-glucan 4-glucanohydrolase
Systematic name: (1→3)-(1→4)-α-D-glucan 4-glucanohydrolase
Comments: Products are nigerose and 4-α-D-nigerosylglucose. No hydrolysis of α-D-glucans containing only 1,3- or 1,4-bonds.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9047-04-5
References:
1.  Tung, K. and Nordin, J.H. Structure of the tetrasaccharide produced by the hydrolysis of nigeran by the enzyme mycodextranase. Biochim. Biophys. Acta 158 (1968) 154–156. [DOI] [PMID: 5652425]
[EC 3.2.1.61 created 1972]
 
 
EC 3.2.1.62     
Accepted name: glycosylceramidase
Reaction: a glycosyl-N-acylsphingosine + H2O = a ceramide + a sugar
For diagram of glycolipid biosynthesis, click here
Glossary: a ceramide = an N-acylsphingosine
Other name(s): phlorizin hydrolase; phloretin-glucosidase; glycosyl ceramide glycosylhydrolase; cerebrosidase; phloridzin β-glucosidase; lactase-phlorizin hydrolase; phloridzin glucosidase
Systematic name: glycosyl-N-acylsphingosine glycohydrolase
Comments: Broad specificity [cf. EC 3.2.1.45 (glucosylceramidase) and EC 3.2.1.46 (galactosylceramidase)]. Also hydrolyses phlorizin to phloretin and glucose. The intestinal enzyme is a complex that also catalyses the reaction of EC 3.2.1.108 lactase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-10-7
References:
1.  Leese, H.J. and Semenza, G. On the identity between the small intestinal enzymes phlorizin hydrolase and glycosylceramidase. J. Biol. Chem. 248 (1973) 8170–8173. [PMID: 4752949]
2.  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. [DOI] [PMID: 5082068]
3.  Malathi, P. and Crane, R.K. Phlorizin hydrolase: a β-glucosidase of hamster intestinal brush border membrane. Biochim. Biophys. Acta 173 (1969) 245–256. [DOI] [PMID: 5774775]
[EC 3.2.1.62 created 1972, modified 1976]
 
 
EC 3.2.1.63     
Accepted name: 1,2-α-L-fucosidase
Reaction: methyl-2-α-L-fucopyranosyl-β-D-galactoside + H2O = L-fucose + methyl β-D-galactoside
Other name(s): almond emulsin fucosidase; α-(1→2)-L-fucosidase
Systematic name: 2-α-L-fucopyranosyl-β-D-galactoside fucohydrolase
Comments: Highly specific for non-reducing terminal L-fucose residues linked to D-galactose residues by a 1,2-α-linkage. Not identical with EC 3.2.1.111 1,3-α-L-fucosidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-45-2
References:
1.  Bahl, O.P. Glycosidases of Aspergillus niger. II. Purification and general properties of 1,2-α-L-fucosidase. J. Biol. Chem. 245 (1970) 299–304. [PMID: 5460888]
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. [DOI] [PMID: 18111]
3.  Reglero, A. and Cabezas, J.A. Glycosidases of molluscs. Purification and properties of α-L-fucosidase from Chamelea gallina L. Eur. J. Biochem. 66 (1976) 379–387. [DOI] [PMID: 7458]
[EC 3.2.1.63 created 1972]
 
 
EC 3.2.1.64     
Accepted name: 2,6-β-fructan 6-levanbiohydrolase
Reaction: Hydrolysis of (2→6)-β-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(β-D-fructofuranosyl)-D-fructose, from the end of the chain
Other name(s): β-2,6-fructan-6-levanbiohydrolase; 2,6-β-D-fructan 6-levanbiohydrolase; levanbiose-producing levanase; 2,6-β-D-fructan 6-β-D-fructofuranosylfructohydrolase
Systematic name: (2→6)-β-D-fructofuranan 6-(β-D-fructosyl)-D-fructose-hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-46-3
References:
1.  Avigad, G. and Zelikson, R. Cleavage of fructans to levanbiose by a specific hydrolase. Bull. Res. Counc. Isr. 11 (1963) 253–257.
2.  Saito, K., Kondo, K., Kojima, I., Yokota, A. and Tomita, F. Purification and characterization of 2,6-β-D-fructan 6-levanbiohydrolase from Streptomyces exfoliatus F3-2. Appl. Environ. Microbiol. 66 (2000) 252–256. [DOI] [PMID: 10618232]
3.  Saito, K., Oda, Y., Tomita, F. and Yokota, A. Molecular cloning of the gene for 2,6-β-D-fructan 6-levanbiohydrolase from Streptomyces exfoliatus F3-2. FEMS Microbiol. Lett. 218 (2003) 265–270. [DOI] [PMID: 12586402]
4.  Song, E.K., Kim, H., Sung, H.K. and Cha, J. Cloning and characterization of a levanbiohydrolase from Microbacterium laevaniformans ATCC 15953. Gene 291 (2002) 45–55. [DOI] [PMID: 12095678]
5.  Kang, E.J., Lee, S.O., Lee, J.D., Lee, T.H. and Lee, T.H. Purification and characterization of a levanbiose-producing levanase from Pseudomonas sp. No. 43. Biotechnol. Appl. Biochem. 29 (1999) 263–268. [PMID: 10334957]
[EC 3.2.1.64 created 1972, modified 2004]
 
 
EC 3.2.1.65     
Accepted name: levanase
Reaction: Random hydrolysis of (2→6)-β-D-fructofuranosidic linkages in (2→6)-β-D-fructans (levans) containing more than 3 fructose units
Other name(s): levan hydrolase; 2,6-β-D-fructan fructanohydrolase
Systematic name: (2→6)-β-D-fructan fructanohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9041-11-6
References:
1.  Avigad, G. and Bauer, S. Fructan hydrolases. Methods Enzymol. 8 (1966) 621–628.
[EC 3.2.1.65 created 1972]
 
 
EC 3.2.1.66     
Accepted name: quercitrinase
Reaction: quercitrin + H2O = L-rhamnose + quercetin
Systematic name: quercitrin 3-L-rhamnohydrolase
Comments: Quercitrin is quercetin 3-L-rhamnoside.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-47-4
References:
1.  Westlake, D.W.S. Microbiological degradation of quercitrin. Can. J. Microbiol. 9 (1963) 211–220.
[EC 3.2.1.66 created 1972]
 
 
EC 3.2.1.67     
Accepted name: galacturonan 1,4-α-galacturonidase
Reaction: [(1→4)-α-D-galacturonide]n + H2O = [(1→4)-α-D-galacturonide]n-1 + D-galacturonate
Other name(s): exo-polygalacturonase; poly(galacturonate) hydrolase (ambiguous); exo-D-galacturonase; exo-D-galacturonanase; exopoly-D-galacturonase; poly(1,4-α-D-galacturonide) galacturonohydrolase (ambiguous); pgaA (gene name); pgaB (gene name); pgaC (gene name); pgaD (gene name); pgaE (gene name); pgaI (gene name); pgaII (gene name); poly[(1→4)-α-D-galacturonide] galacturonohydrolase; galacturan 1,4-α-galacturonidase (incorrect)
Systematic name: poly[(1→4)-α-D-galacturonide] non-reducing-end galacturonohydrolase
Comments: The enzyme hydrolyses the first glycosidic bond from the non-reducing end of the substrate. It is specific for saturated oligomers of D-homogalacturonan, and is unable to degrade unsaturated substrates or methyl-esterified substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9045-35-6
References:
1.  Hasegawa, H. and Nagel, C.W. Isolation of an oligogalacturonate hydrolase from a Bacillus species. Arch. Biochem. Biophys. 124 (1968) 513–520. [DOI] [PMID: 5661621]
2.  Kluskens, L.D., van Alebeek, G.J., Walther, J., Voragen, A.G., de Vos, W.M. and van der Oost, J. Characterization and mode of action of an exopolygalacturonase from the hyperthermophilic bacterium Thermotoga maritima. FEBS J. 272 (2005) 5464–5473. [PMID: 16262687]
3.  Martens-Uzunova, E.S., Zandleven, J.S., Benen, J.A., Awad, H., Kools, H.J., Beldman, G., Voragen, A.G., Van den Berg, J.A. and Schaap, P.J. A new group of exo-acting family 28 glycoside hydrolases of Aspergillus niger that are involved in pectin degradation. Biochem. J. 400 (2006) 43–52. [PMID: 16822232]
4.  Pijning, T., van Pouderoyen, G., Kluskens, L., van der Oost, J. and Dijkstra, B.W. The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer. FEBS Lett. 583 (2009) 3665–3670. [PMID: 19854184]
[EC 3.2.1.67 created 1972, modified 2019]
 
 
EC 3.2.1.68     
Accepted name: isoamylase
Reaction: Hydrolysis of (1→6)-α-D-glucosidic branch linkages in glycogen, amylopectin and their β-limit dextrins
Glossary: pullulan = a linear polymer of (1→6)-linked maltotriose units
Other name(s): debranching enzyme; glycogen α-1,6-glucanohydrolase
Systematic name: glycogen 6-α-D-glucanohydrolase
Comments: Also readily hydrolyses amylopectin. Differs from EC 3.2.1.41 (pullulanase) and EC 3.2.1.142 (limit dextrinase) by its inability to hydrolyse pullulan, and by limited action on α-limit dextrins. Maltose is the smallest sugar it can release from an α-(1→6)-linkage.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-73-6
References:
1.  Yokobayashi, K., Misaki, A. and Harada, T. Purification and properties of Pseudomonas isoamylase. Biochim. Biophys. Acta 212 (1970) 458–469. [DOI] [PMID: 5456995]
[EC 3.2.1.68 created 1972, modified 1976, modified 2000]
 
 
EC 3.2.1.69      
Deleted entry:  amylopectin 6-glucanohydrolase. Now included with EC 3.2.1.41 pullulanase
[EC 3.2.1.69 created 1972, deleted 1976]
 
 
EC 3.2.1.70     
Accepted name: glucan 1,6-α-glucosidase
Reaction: Hydrolysis of (1→6)-α-D-glucosidic linkages in (1→6)-α-D-glucans and derived oligosaccharides
Other name(s): exo-1,6-β-glucosidase; glucodextrinase; glucan α-1,6-D-glucohydrolase
Systematic name: glucan 6-α-D-glucohydrolase
Comments: Hydrolysis is accompanied by inversion at C-1, so that new reducing ends are released in the β-configuration. Dextrans and isomaltosaccharides are hydrolysed, as is isomaltose, but very slowly. The enzyme from some sources also possesses the activity of EC 3.2.1.59 (glucan endo-1,3-α-glucosidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-48-5
References:
1.  Ohya, T., Sawai, T., Uemura, S. and Abe, K. Some catalytic properties of an exo-1,6-α-glucosidase (glucodextranase) from Arthrobacter globiformis I42. Agric. Biol. Chem. 42 (1978) 571–577.
2.  Sawai, T., Yamaki, T. and Ohya, T. Preparation and some properties of Arthrobacter globiformis exo-1,6-α-glucosidase. Agric. Biol. Chem. 40 (1976) 1293–1299.
3.  Walker, G.J. and Pulkownik, A. Degradation of dextrans by an α-1,6-glucan glucohydrolase from Streptococcus mitis. Carbohydr. Res. 29 (1973) 1–14. [DOI] [PMID: 4356399]
[EC 3.2.1.70 created 1972, modified 2001]
 
 
EC 3.2.1.71     
Accepted name: glucan endo-1,2-β-glucosidase
Reaction: Random hydrolysis of (1→2)-glucosidic linkages in (1→2)-β-D-glucans
Other name(s): endo-1,2-β-glucanase; β-D-1,2-glucanase; endo-(1→2)-β-D-glucanase; 1,2-β-D-glucan glucanohydrolase
Systematic name: 2-β-D-glucan glucanohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-49-6
References:
1.  Reese, E.T., Parrish, F.W. and Mandels, M. β-D-1,2-Glucanases in fungi. Can. J. Microbiol. 7 (1961) 309–317. [PMID: 13740314]
[EC 3.2.1.71 created 1972]
 
 
EC 3.2.1.72     
Accepted name: xylan 1,3-β-xylosidase
Reaction: Hydrolysis of successive xylose residues from the non-reducing termini of (1→3)-β-D-xylans
Other name(s): 1,3-β-D-xylosidase; exo-1,3-β-xylosidase; β-1,3′-xylanase; exo-β-1,3′-xylanase; 1,3-β-D-xylan xylohydrolase
Systematic name: 3-β-D-xylan xylohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-50-9
References:
1.  Fukui, S., Suzuki, T., Kitahara, K. and Miwa, T. β-1,3′-Xylanase. J. Gen. Appl. Microbiol. 6 (1960) 270–282.
[EC 3.2.1.72 created 1972]
 
 
EC 3.2.1.73     
Accepted name: licheninase
Reaction: Hydrolysis of (1→4)-β-D-glucosidic linkages in β-D-glucans containing (1→3)- and (1→4)-bonds
Other name(s): lichenase; β-(1→4)-D-glucan 4-glucanohydrolase; 1,3;1,4-β-glucan endohydrolase; 1,3;1,4-β-glucan 4-glucanohydrolase; 1,3-1,4-β-D-glucan 4-glucanohydrolase
Systematic name: (1→3)-(1→4)-β-D-glucan 4-glucanohydrolase
Comments: Acts on lichenin and cereal β-D-glucans, but not on β-D-glucans containing only 1,3- or 1,4-bonds.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-51-0
References:
1.  Barras, D.R., Moore, A.E. and Stone, B.A. Enzyme-substrate relations among β-glucan hydrolases. Adv. Chem. Ser. 95 (1969) 105–138.
[EC 3.2.1.73 created 1972]
 
 
EC 3.2.1.74     
Accepted name: glucan 1,4-β-glucosidase
Reaction: Hydrolysis of (1→4)-linkages in (1→4)-β-D-glucans, to remove successive glucose units
Other name(s): exo-1,4-β-glucosidase; exocellulase; exo-β-1,4-glucosidase; exo-β-1,4-glucanase; β-1,4-β-glucanase; β-glucosidase; exo-1,4-β-glucanase; 1,4-β-D-glucan glucohydrolase
Systematic name: 4-β-D-glucan glucohydrolase
Comments: Acts on 1,4-β-D-glucans and related oligosaccharides. Cellobiose is hydrolysed, but very slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-52-1
References:
1.  Barras, D.R., Moore, A.E. and Stone, B.A. Enzyme-substrate relations among β-glucan hydrolases. Adv. Chem. Ser. 95 (1969) 105–138.
[EC 3.2.1.74 created 1972]
 
 
EC 3.2.1.75     
Accepted name: glucan endo-1,6-β-glucosidase
Reaction: Random hydrolysis of (1→6)-linkages in (1→6)-β-D-glucans
Other name(s): endo-1,6-β-glucanase; β-1→6)-β-D-glucanase; β-1,6-glucanase-pustulanase; β-1,6-glucan hydrolase; β-1,6-glucan 6-glucanohydrolase; 1,6-β-D-glucan glucanohydrolase
Systematic name: 6-β-D-glucan glucanohydrolase
Comments: Acts on lutean, pustulan and 1,6-oligo-β-D-glucosides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37278-39-0
References:
1.  Reese, E.T., Parrish, F.W. and Mandels, M. β-D-1,6-Glucanases in fungi. Can. J. Microbiol. 8 (1962) 327–334. [PMID: 14491003]
[EC 3.2.1.75 created 1972]
 
 
EC 3.2.1.76     
Accepted name: L-iduronidase
Reaction: Hydrolysis of unsulfated α-L-iduronosidic linkages in dermatan sulfate
Other name(s): α-L-iduronidase
Systematic name: glycosaminoglycan α-L-iduronohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9073-56-7
References:
1.  Matalon, R., Cifonelli, J.A. and Dorfman, A. L-Iduronidase in cultured human fibroblasts and liver. Biochem. Biophys. Res. Commun. 42 (1971) 340–345. [DOI] [PMID: 4993544]
2.  Rome, L.H., Garvin, A.J. and Neufeld, E.F. Human kidney α-L-iduronidase: purification and characterization. Arch. Biochem. Biophys. 189 (1978) 344–353. [DOI] [PMID: 30407]
3.  Srivastava, R.M., Hudson, N., Seymour, F.R. and Weissman, B. Preparation of (aryl α-L-idopyranosid)uronic acids. Carbohydr. Res. 60 (1978) 315–326.
[EC 3.2.1.76 created 1972]
 
 
EC 3.2.1.77     
Accepted name: mannan 1,2-(1,3)-α-mannosidase
Reaction: Hydrolysis of (1→2)- and (1→3)-linkages in yeast mannan, releasing mannose
Other name(s): exo-1,2-1,3-α-mannosidase; 1,2-1,3-α-D-mannan mannohydrolase
Systematic name: (1→2)-(1→3)-α-D-mannan mannohydrolase
Comments: A 1,6-α-D-mannan backbone remains after action on yeast mannan. This is further attacked, but slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-53-2
References:
1.  Jones, G.H. and Ballou, C.E. Studies on the structure of yeast mannan. I. Purification and some properties of an α-mannosidase from an Arthrobacter species. J. Biol. Chem. 244 (1969) 1043–1051. [PMID: 5769177]
2.  Jones, G.H. and Ballou, C.E. Studies on the structure of yeast mannan. II. Mode of action of the Arthrobacter α-mannosidase on yeast mannan. J. Biol. Chem. 244 (1969) 1052–1059. [PMID: 5814027]
[EC 3.2.1.77 created 1972]
 
 
EC 3.2.1.78     
Accepted name: mannan endo-1,4-β-mannosidase
Reaction: Random hydrolysis of (1→4)-β-D-mannosidic linkages in mannans, galactomannans and glucomannans
Other name(s): endo-1,4-β-mannanase; endo-β-1,4-mannase; β-mannanase B; β-1,4-mannan 4-mannanohydrolase; endo-β-mannanase; β-D-mannanase; 1,4-β-D-mannan mannanohydrolase
Systematic name: 4-β-D-mannan mannanohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-54-3
References:
1.  Eriksson, A.F.V. Purification and characterisation of a fungal β-mannanase. Acta Chem. Scand. 22 (1968) 1924–1934.
2.  Reese, E.T. β-Mannanases of fungi. Can. J. Microbiol. 11 (1965) 167–183. [PMID: 14323029]
[EC 3.2.1.78 created 1972]
 
 
EC 3.2.1.79      
Deleted entry:  α-L-arabinofuranoside hydrolase. Now included with EC 3.2.1.55 α-N-arabinofuranosidase
[EC 3.2.1.79 created 1972, deleted 1976]
 
 
EC 3.2.1.80     
Accepted name: fructan β-fructosidase
Reaction: Hydrolysis of terminal, non-reducing (2→1)- and (2→6)-linked β-D-fructofuranose residues in fructans
For diagram of hydrolysis of the 2,6-bond, click here and the 2,1-bond, click here
Other name(s): exo-β-D-fructosidase; exo-β-fructosidase; polysaccharide β-fructofuranosidase; fructan exohydrolase
Systematic name: β-D-fructan fructohydrolase
Comments: Hydrolyses inulin and levan, and also sucrose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-56-5
References:
1.  DaCosta, T. and Gibbons, R.J. Hydrolysis of levan by human plaque streptococci. Arch. Oral Biol. 13 (1968) 609–617. [PMID: 5244285]
2.  Jacques, N.J., Morrey-Jones, J.G. and Walker, G.J. Inducible and constitutive formation of fructanase in batch and continuous cultures of Streptococcus mutans. J. Gen. Microbiol. 131 (1985) 1625–1633. [DOI] [PMID: 4045423]
[EC 3.2.1.80 created 1972]
 
 
EC 3.2.1.81     
Accepted name: β-agarase
Reaction: Hydrolysis of (1→4)-β-D-galactosidic linkages in agarose, giving the tetramer as the predominant product
Glossary: agarose = a linear polysaccharide produced by some members of the Rhodophyta (red algae) made up from alternating D-galactose and 3,6-anhydro-α-L-galactopyranose residues joined by α-(1→3)- and β-(1→4)-linkages. In the field of oligosaccharides derived from agarose, carrageenans, etc., in which alternate residues are 3,6-anhydro sugars, the prefix ’neo’ designates an oligosaccharide whose non-reducing end is the anhydro sugar, and the absence of this prefix means that it is not.
For example:
neoagarobiose = 3,6-anhydro-α-L-galactopyranosyl-(1→3)-D-galactose
agarobiose = β-D-galactopyranosyl-(1→4)-3,6-anhydro-L-galactose
Other name(s): agarase (ambiguous); AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase (incorrect)
Systematic name: agarose 4-glycanohydrolase
Comments: Also acts on porphyran, but more slowly [1]. This enzyme cleaves the β-(1→4) linkages of agarose in a random manner with retention of the anomeric-bond configuration, producing β-anomers that give rise progressively to α-anomers when mutarotation takes place [6]. The end products of hydrolysis are neoagarotetraose and neoagarohexaose in the case of AgaA from the marine bacterium Zobellia galactanivorans, and neoagarotetraose and neoagarobiose in the case of AgaB [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-57-6
References:
1.  Duckworth, M. and Turvey, J.R. The action of a bacterial agarase on agarose, porphyran and alkali-treated porphyran. Biochem. J. 113 (1969) 687–692. [PMID: 5386190]
2.  Allouch, J., Jam, M., Helbert, W., Barbeyron, T., Kloareg, B., Henrissat, B. and Czjzek, M. The three-dimensional structures of two β-agarases. J. Biol. Chem. 278 (2003) 47171–47180. [DOI] [PMID: 12970344]
3.  Ohta, Y., Nogi, Y., Miyazaki, M., Li, Z., Hatada, Y., Ito, S. and Horikoshi, K. Enzymatic properties and nucleotide and amino acid sequences of a thermostable β-agarase from the novel marine isolate, JAMB-A94. Biosci. Biotechnol. Biochem. 68 (2004) 1073–1081. [DOI] [PMID: 15170112]
4.  Ohta, Y., Hatada, Y., Nogi, Y., Miyazaki, M., Li, Z., Akita, M., Hidaka, Y., Goda, S., Ito, S. and Horikoshi, K. Enzymatic properties and nucleotide and amino acid sequences of a thermostable β-agarase from a novel species of deep-sea Microbulbifer. Appl. Microbiol. Biotechnol. 64 (2004) 505–514. [DOI] [PMID: 15088129]
5.  Sugano, Y., Terada, I., Arita, M., Noma, M. and Matsumoto, T. Purification and characterization of a new agarase from a marine bacterium, Vibrio sp. strain JT0107. Appl. Environ. Microbiol. 59 (1993) 1549–1554. [PMID: 8517750]
6.  Jam, M., Flament, D., Allouch, J., Potin, P., Thion, L., Kloareg, B., Czjzek, M., Helbert, W., Michel, G. and Barbeyron, T. The endo-β-agarases AgaA and AgaB from the marine bacterium Zobellia galactanivorans: two paralogue enzymes with different molecular organizations and catalytic behaviours. Biochem. J. 385 (2005) 703–713. [DOI] [PMID: 15456406]
[EC 3.2.1.81 created 1972, modified 2006]
 
 
EC 3.2.1.82     
Accepted name: exo-poly-α-digalacturonosidase
Reaction: [(1→4)-α-D-galacturonosyl]n + H2O = α-D-galacturonosyl-(1→4)-D-galacturonate + [(1→4)-α-D-galacturonosyl]n-2
Other name(s): pehX (gene name); poly(1,4-α-D-galactosiduronate) digalacturonohydrolase; exopolygalacturonosidase (misleading); poly[(1→4)-α-D-galactosiduronate] digalacturonohydrolase; exo-poly-α-galacturonosidase
Systematic name: poly[(1→4)-α-D-galactosiduronate] non-reducing-end-digalacturonohydrolase
Comments: The enzyme, characterized from bacteria, hydrolyses the second α-1,4-glycosidic bond from the non-reducing end of polygalacturonate, releasing digalacturonate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-58-7
References:
1.  Hasegawa, H. and Nagel, C.W. Isolation of an oligogalacturonate hydrolase from a Bacillus species. Arch. Biochem. Biophys. 124 (1968) 513–520. [DOI] [PMID: 5661621]
2.  Hatanaka, C. and Ozawa, J. Enzymic degradation of pectic acid. XIII. New exopolygalacturonase producing digalacturonic acid from pectic acid. J. Agric. Chem. Soc. Jpn.. 43 (1968) 764–772.
3.  Hatanaka, C. and Ozawa, J. Ber. des O'Hara Inst. 15 (1971) 47.
4.  He, S.Y. and Collmer, A. Molecular cloning, nucleotide sequence, and marker exchange mutagenesis of the exo-poly-α-D-galacturonosidase-encoding pehX gene of Erwinia chrysanthemi EC16. J. Bacteriol. 172 (1990) 4988–4995. [PMID: 2168372]
[EC 3.2.1.82 created 1972, modified 2019]
 
 
EC 3.2.1.83     
Accepted name: κ-carrageenase
Reaction: Endohydrolysis of (1→4)-β-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in κ-carrageenans
For diagram of reaction, click here
Glossary: In the field of oligosaccharides derived from agarose, carrageenans, etc., in which alternate residues are 3,6-anhydro sugars, the prefix ’neo’ designates an oligosaccharide whose non-reducing end is the anhydro sugar, and the absence of this prefix means that it is not.
For example:
ι-neocarrabiose = 3,6-anhydro-2-O-sulfo-α-D-galactopyranosyl-(1→3)-4-O-sulfo-D-galactose
ι-carrabiose = 4-O-sulfo- β-D-galactopyranosyl-(1→4)-3,6-anhydro-2-O-sulfo-D-galactose
Other name(s): κ-carrageenan 4-β-D-glycanohydrolase
Systematic name: κ-carrageenan 4-β-D-glycanohydrolase (configuration-retaining)
Comments: The main products of hydrolysis are neocarrabiose-sulfate and neocarratetraose-sulfate [5]. Unlike EC 3.2.1.157 (ι-carrageenase), but similar to EC 3.2.1.81 (β-agarase), this enzyme proceeds with retention of the anomeric configuration.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-59-8
References:
1.  Weigl, J. and Yashe, W. The enzymic hydrolysis of carrageenan by Pseudomonas carrageenovora: purification of a κ-carrageenase. Can. J. Microbiol. 12 (1966) 939–947. [PMID: 5972647]
2.  Potin, P., Sanseau, A., Le Gall, Y., Rochas, C. and Kloareg, B. Purification and characterization of a new κ-carrageenase from a marine Cytophaga-like bacterium. Eur. J. Biochem. 201 (1991) 241–247. [DOI] [PMID: 1915370]
3.  Potin, P., Richard, C., Barbeyron, T., Henrissat, B., Gey, C., Petillot, Y., Forest, E., Dideberg, O., Rochas, C. and Kloareg, B. Processing and hydrolytic mechanism of the cgkA-encoded κ-carrageenase of Alteromonas carrageenovora. Eur. J. Biochem. 228 (1995) 971–975. [DOI] [PMID: 7737202]
4.  Michel, G., Barbeyron, T., Flament, D., Vernet, T., Kloareg, B. and Dideberg, O. Expression, purification, crystallization and preliminary x-ray analysis of the κ-carrageenase from Pseudoalteromonas carrageenovora. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 918–920. [PMID: 10089334]
5.  Michel, G., Chantalat, L., Duee, E., Barbeyron, T., Henrissat, B., Kloareg, B. and Dideberg, O. The κ-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases. Structure 9 (2001) 513–525. [DOI] [PMID: 11435116]
[EC 3.2.1.83 created 1972, modified 2006]
 
 
EC 3.2.1.84     
Accepted name: glucan 1,3-α-glucosidase
Reaction: Hydrolysis of terminal (1→3)-α-D-glucosidic links in (1→3)-α-D-glucans
Other name(s): exo-1,3-α-glucanase; glucosidase II; 1,3-α-D-glucan 3-glucohydrolase
Systematic name: 3-α-D-glucan 3-glucohydrolase
Comments: Does not act on nigeran.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9073-99-8
References:
1.  Zonneveld, B.J.M. A new type of enzyme, and exo-splitting α-1,3 glucanase from non-induced cultures of Aspergillus nidulans. Biochim. Biophys. Acta 258 (1972) 541–547. [DOI] [PMID: 4622000]
[EC 3.2.1.84 created 1972]
 
 
EC 3.2.1.85     
Accepted name: 6-phospho-β-galactosidase
Reaction: a 6-phospho-β-D-galactoside + H2O = 6-phospho-D-galactose + an alcohol
Other name(s): phospho-β-galactosidase; β-D-phosphogalactoside galactohydrolase; phospho-β-D-galactosidase; 6-phospho-β-D-galactosidase
Systematic name: 6-phospho-β-D-galactoside 6-phosphogalactohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37237-42-6
References:
1.  Hengstenberg, W., Penberthy, W.K. and Morse, M.L. Purification of the staphylococcal 6-phospho-β-D-galactosidase. Eur. J. Biochem. 14 (1970) 27–32. [DOI] [PMID: 5447434]
[EC 3.2.1.85 created 1976]
 
 
EC 3.2.1.86     
Accepted name: 6-phospho-β-glucosidase
Reaction: 6-phospho-β-D-glucosyl-(1→4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate
Other name(s): phospho-β-glucosidase A; phospho-β-glucosidase; phosphocellobiase; 6-phospho-β-D-glucosyl-(1,4)-D-glucose glucohydrolase
Systematic name: 6-phospho-β-D-glucosyl-(1→4)-D-glucose glucohydrolase
Comments: Also hydrolyses several other phospho-β-D-glucosides, but not their non-phosphorylated forms.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37205-51-9
References:
1.  Palmer, R.E. and Anderson, R.L. Cellobiose metabolism in Aerobacter aerogenes. 3. Cleavage of cellobiose monophosphate by a phospho-β-glucosidase. J. Biol. Chem. 247 (1972) 3420–3423. [PMID: 4624114]
[EC 3.2.1.86 created 1976]
 
 
EC 3.2.1.87     
Accepted name: capsular-polysaccharide endo-1,3-α-galactosidase
Reaction: Random hydrolysis of (1→3)-α-D-galactosidic linkages in Aerobacter aerogenes capsular polysaccharide
Other name(s): polysaccharide depolymerase; capsular polysaccharide galactohydrolase
Systematic name: Aerobacter-capsular-polysaccharide galactohydrolase
Comments: Hydrolyses the galactosyl-α-1,3-D-galactose linkages only in the complex substrate, bringing about depolymerization.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-16-5
References:
1.  Yurewicz, E.C., Ghalambor, M.A., Duckworth, D.H. and Heath, E.C. Catalytic and molecular properties of a phage-induced capsular polysaccharide depolymerase. J. Biol. Chem. 246 (1971) 5607–5716. [PMID: 5096084]
2.  Yurewicz, E.C., Ghalambor, M.A. and Heath, E.C. The structure of Aerobacter aerogenes capsular polysaccharide. J. Biol. Chem. 246 (1971) 5596–5606. [PMID: 4328830]
[EC 3.2.1.87 created 1976]
 
 
EC 3.2.1.88     
Accepted name: non-reducing end β-L-arabinopyranosidase
Reaction: Removal of a terminal β-L-arabinopyranose residue from the non-reducing end of its substrate.
Other name(s): vicianosidase; β-L-arabinosidase (ambiguous); β-L-arabinoside arabinohydrolase (ambiguous)
Systematic name: β-L-arabinopyranoside non-reducing end β-L-arabinopyranosidase
Comments: The enzyme, which was characterized from dormant seeds of the plant Cajanus cajan (pigeon pea), has been shown to remove the terminal non-reducing β-L-arabinopyranoside residue from the artificial substrate p-nitrophenyl-β-L-arabinopyranose [1]. In the presence of methanol the enzyme demonstrates transglycosylase activity, transferring the arabinose moiety to methanol while retaining the anomeric configuration, generating 1-O-methyl-β-L-arabinopyranose [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39361-63-2
References:
1.  Dey, P.M. β-L-Arabinosidase from Cajanus indicus: a new enzyme. Biochim. Biophys. Acta 302 (1973) 393–398. [DOI] [PMID: 4699248]
2.  Dey, P. M. Further characterization of β-L-arabinosidase from Cajanus indicus. Biochim.Biophys. Acta 746 (1983) 8–13.
[EC 3.2.1.88 created 1976, modified 2013]
 
 
EC 3.2.1.89     
Accepted name: arabinogalactan endo-β-1,4-galactanase
Reaction: The enzyme specifically hydrolyses (1→4)-β-D-galactosidic linkages in type I arabinogalactans.
Other name(s): endo-1,4-β-galactanase; galactanase (ambiguous); arabinogalactanase; ganB (gene name)
Systematic name: arabinogalactan 4-β-D-galactanohydrolase
Comments: This enzyme, isolated from the bacterium Bacillus subtilis, hydrolyses the β(1→4) bonds found in type I plant arabinogalactans, which are a component of the primary cell walls of dicots. The predominant product is a tetrasaccharide. cf. EC 3.2.1.181, galactan endo-β-1,3-galactanase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 58182-40-4
References:
1.  Emi, S. and Yamamoto, T. Purification and properties of several galactanases of Bacillus subtilis var. amylosacchariticus. Agric. Biol. Chem. 36 (1972) 1945–1954.
2.  Labavitch, J.M., Freeman, L.E. and Albersheim, P. Structure of plant cell walls. Purification and characterization of a β-1,4-galactanase which degrades a structural component of the primary cell walls of dicots. J. Biol. Chem. 251 (1976) 5904–5910. [PMID: 823153]
3.  Shipkowski, S. and Brenchley, J.E. Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 β-galactosidases are arabinogalactan type I oligomer hydrolases. Appl. Environ. Microbiol. 72 (2006) 7730–7738. [DOI] [PMID: 17056685]
[EC 3.2.1.89 created 1976, modified 2012]
 
 
EC 3.2.1.90      
Deleted entry:  arabinogalactan endo-1,3-β-galactosidase. The enzyme was not sufficiently characterized to warrant an EC number
[EC 3.2.1.90 created 1976, deleted 2001]
 
 
EC 3.2.1.91     
Accepted name: cellulose 1,4-β-cellobiosidase (non-reducing end)
Reaction: Hydrolysis of (1→4)-β-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
Other name(s): exo-cellobiohydrolase; β-1,4-glucan cellobiohydrolase; β-1,4-glucan cellobiosylhydrolase; 1,4-β-glucan cellobiosidase; exoglucanase; avicelase; CBH 1; C1 cellulase; cellobiohydrolase I; cellobiohydrolase; exo-β-1,4-glucan cellobiohydrolase; 1,4-β-D-glucan cellobiohydrolase; cellobiosidase
Systematic name: 4-β-D-glucan cellobiohydrolase (non-reducing end)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37329-65-0
References:
1.  Berghem, L.E.R. and Pettersson, L.G. The mechanism of enzymatic cellulose degradation. Purification of a cellulolytic enzyme from Trichoderma viride active on highly ordered cellulose. Eur. J. Biochem. 37 (1973) 21–30. [DOI] [PMID: 4738092]
2.  Eriksson, K.E. and Pettersson, B. Extracellular enzyme system utilized by the fungus Sporotrichum pulverulentum (Chrysosporium lignorum) for the breakdown of cellulose. 3. Purification and physico-chemical characterization of an exo-1,4-β-glucanase. Eur. J. Biochem. 51 (1975) 213–218. [DOI] [PMID: 235428]
3.  Halliwell, G., Griffin, M. and Vincent, R. The role of component C1 in cellulolytic systems. Biochem. J. 127 (1972) 43P. [PMID: 5076675]
[EC 3.2.1.91 created 1976, modified 2011]
 
 
EC 3.2.1.92     
Accepted name: peptidoglycan β-N-acetylmuramidase
Reaction: Hydrolysis of terminal, non-reducing N-acetylmuramic residues
Other name(s): exo-β-N-acetylmuramidase; exo-β-acetylmuramidase; β-2-acetamido-3-O-(D-1-carboxyethyl)-2-deoxy-D-glucoside acetamidodeoxyglucohydrolase
Systematic name: peptidoglycan β-N-acetylmuramoylexohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52219-03-1
References:
1.  Del Rio, L.A. and Berkeley, R.C.W. Exo-β-N-acetylmuramidase - a novel hexosaminidase. Production by Bacillus subtilis B, purification and characterization. Eur. J. Biochem. 65 (1976) 3–12. [DOI] [PMID: 6281]
[EC 3.2.1.92 created 1976]
 
 
EC 3.2.1.93     
Accepted name: α,α-phosphotrehalase
Reaction: α,α-trehalose 6-phosphate + H2O = D-glucose + D-glucose 6-phosphate
Other name(s): phosphotrehalase
Systematic name: α,α-trehalose-6-phosphate phosphoglucohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 54576-93-1
References:
1.  Bhumiratana, A., Anderson, R.L. and Costilow, R.N. Trehalose metabolism by Bacillus popilliae. J. Bacteriol. 119 (1974) 484–493. [PMID: 4369400]
[EC 3.2.1.93 created 1976]
 
 
EC 3.2.1.94     
Accepted name: glucan 1,6-α-isomaltosidase
Reaction: Hydrolysis of (1→6)-α-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains
Other name(s): exo-isomaltohydrolase; isomalto-dextranase; isomaltodextranase; G2-dextranase; 1,6-α-D-glucan isomaltohydrolase
Systematic name: 6-α-D-glucan isomaltohydrolase
Comments: Optimum activity is on those 1,6-α-D-glucans containing 6, 7 and 8 glucose units; those containing 3, 4 and 5 glucose units are hydrolysed at slower rates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 56467-68-6
References:
1.  Sawai, T., Toriyama, K. and Yano, K. A bacterial dextranase releasing only isomaltose from dextrans. J. Biochem. (Tokyo) 75 (1974) 105–112. [PMID: 4826536]
2.  Sawai, T. and Niwa, Y. Transisomaltosylation activity of a bacterial isomaltodextranase. Agric. Biol. Chem. 39 (1975) 1077–1083.
[EC 3.2.1.94 created 1976]
 
 
EC 3.2.1.95     
Accepted name: dextran 1,6-α-isomaltotriosidase
Reaction: Hydrolysis of (1→6)-α-D-glucosidic linkages in dextrans, to remove successive isomaltotriose units from the non-reducing ends of the chains
Other name(s): exo-isomaltotriohydrolase; 1,6-α-D-glucan isomaltotriohydrolase
Systematic name: 6-α-D-glucan isomaltotriohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72561-11-6
References:
1.  Sugiura, M., Ito, A. and Yamaguchi, T. Studies on dextranase. II. New exo-dextranase from Brevibacterium fuscum var. Dextranlyticum. Biochim. Biophys. Acta 350 (1974) 61–70. [DOI] [PMID: 4210084]
[EC 3.2.1.95 created 1978]
 
 
EC 3.2.1.96     
Accepted name: mannosyl-glycoprotein endo-β-N-acetylglucosaminidase
Reaction: Endohydrolysis of the N,N′-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact
Other name(s): N,N′-diacetylchitobiosyl β-N-acetylglucosaminidase; endo-β-N-acetylglucosaminidase; mannosyl-glycoprotein endo-β-N-acetylglucosamidase; di-N-acetylchitobiosyl β-N-acetylglucosaminidase; endo-β-acetylglucosaminidase; endo-β-(1→4)-N-acetylglucosaminidase; mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-D-glycohydrolase; endoglycosidase S; endo-N-acetyl-β-D-glucosaminidase; endo-N-acetyl-β-glucosaminidase; endo-β-N-acetylglucosaminidase D; endo-β-N-acetylglucosaminidase F; endo-β-N-acetylglucosaminidase H; endo-β-N-acetylglucosaminidase L; glycopeptide-D-mannosyl-4-N-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase; endoglycosidase H
Systematic name: glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase
Comments: A group of related enzymes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-88-9
References:
1.  Chien, S., Weinburg, R., Li, S. and Li, Y. Endo-β-N-acetylglucosaminidase from fig latex. Biochem. Biophys. Res. Commun. 76 (1977) 317–323.
2.  Koide, N. and Muramatsu, T. Endo-β-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae. J. Biol. Chem. 249 (1974) 4897–4904. [PMID: 4152561]
3.  Pierce, R.J., Spik, G. and Montreuil, J. Cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity in rat liver and kidney. Biochem. J. 180 (1979) 673. [PMID: 486141]
4.  Pierce, R.J., Spik, G. and Montreuil, J. Demonstration and cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver. Biochem. J. 185 (1980) 261–264. [PMID: 7378051]
5.  Tai, T., Yamashita, K., Ogata-Arakawa, M., Koide, N., Muramatsu, T., Iwashita, S., Inoue, Y. and Kobata, A. Structural studies of two ovalbumin glycopeptides in relation to the endo-β-N-acetylglucosaminidase specificity. J. Biol. Chem. 250 (1975) 8569–8575. [PMID: 389]
6.  Tarentino, A.L., Plummer, T.H., Jr. and Maley, F. The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosaminidase H. J. Biol. Chem. 249 (1974) 818–824. [PMID: 4204553]
[EC 3.2.1.96 created 1978]
 
 
EC 3.2.1.97     
Accepted name: endo-α-N-acetylgalactosaminidase
Reaction: β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-[glycoprotein]-L-serine/L-threonine + H2O = β-D-galactosyl-(1→3)-N-acetyl-D-galactosamine + [glycoprotein]-L-serine/L-threonine
Other name(s): endo-α-acetylgalactosaminidase; endo-α-N-acetyl-D-galactosaminidase; mucinaminylserine mucinaminidase; D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase; endo-α-GalNAc-ase; glycopeptide α-N-acetylgalactosaminidase; D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
Systematic name: glycopeptide-D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
Comments: The enzyme catalyses the liberation of Gal-(1→3)-β-GalNAc α-linked to serine or threonine residues of mucin-type glycoproteins. EngBF from the bacterium Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1→3)-β-GalNAc. The enzymes from the bacteria Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. they can also release the core 2 trisaccharide Gal-(1→3)-β-(GlcNAc-(1→6)-β)-GalNAc or the core 3 disaccharide GlcNAc-(1→3)-β-GalNAc) [1,2]. The enzyme may play an important role in the degradation and utilization of mucins having core 1 O-glycan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 59793-96-3
References:
1.  Ashida, H., Maki, R., Ozawa, H., Tani, Y., Kiyohara, M., Fujita, M., Imamura, A., Ishida, H., Kiso, M. and Yamamoto, K. Characterization of two different endo-α-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens. Glycobiology 18 (2008) 727–734. [DOI] [PMID: 18559962]
2.  Koutsioulis, D., Landry, D. and Guthrie, E.P. Novel endo-α-N-acetylgalactosaminidases with broader substrate specificity. Glycobiology 18 (2008) 799–805. [DOI] [PMID: 18635885]
3.  Fujita, K., Oura, F., Nagamine, N., Katayama, T., Hiratake, J., Sakata, K., Kumagai, H. and Yamamoto, K. Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-α-N-acetylgalactosaminidase from Bifidobacterium longum. J. Biol. Chem. 280 (2005) 37415–37422. [DOI] [PMID: 16141207]
4.  Suzuki, R., Katayama, T., Kitaoka, M., Kumagai, H., Wakagi, T., Shoun, H., Ashida, H., Yamamoto, K. and Fushinobu, S. Crystallographic and mutational analyses of substrate recognition of endo-α-N-acetylgalactosaminidase from Bifidobacterium longum. J. Biochem. 146 (2009) 389–398. [DOI] [PMID: 19502354]
5.  Gregg, K.J. and Boraston, A.B. Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of a family 101 glycoside hydrolase from Streptococcus pneumoniae. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 (2009) 133–135. [DOI] [PMID: 19194003]
6.  Ashida, H., Yamamoto, K., Murata, T., Usui, T. and Kumagai, H. Characterization of endo-α-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity. Arch. Biochem. Biophys. 373 (2000) 394–400. [DOI] [PMID: 10620364]
7.  Goda, H.M., Ushigusa, K., Ito, H., Okino, N., Narimatsu, H. and Ito, M. Molecular cloning, expression, and characterization of a novel endo-α-N-acetylgalactosaminidase from Enterococcus faecalis. Biochem. Biophys. Res. Commun. 375 (2008) 441–446. [DOI] [PMID: 18725192]
[EC 3.2.1.97 created 1978 (EC 3.2.1.110 created 1984, incorporated 2008), modified 2008, modified 2011]
 
 
EC 3.2.1.98     
Accepted name: glucan 1,4-α-maltohexaosidase
Reaction: Hydrolysis of (1→4)-α-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends
Other name(s): exo-maltohexaohydrolase; 1,4-α-D-glucan maltohexaohydrolase
Systematic name: 4-α-D-glucan maltohexaohydrolase
Comments: cf. EC 3.2.1.3 glucan 1,4-α-glucosidase, which removes successive glucose residues; EC 3.2.1.2 β-amylase, which removes successive maltose residues; EC 3.2.1.116 glucan 1,4-α-maltotriohydrolase, which removes successive maltotriose units and EC 3.2.1.60 glucan 1,4-α-maltotetraohydrolase, which removes successive maltotetraose residues. The products have the α-configuration.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 72561-12-7
References:
1.  Kainuma, K., Wako, K., Kobayashi, A., Nogami, A. and Suzuki, S. Purification and some properties of a novel maltohexaose-producing exo-amylase from Aerobacter aerogenes. Biochim. Biophys. Acta 410 (1975) 333–346. [DOI] [PMID: 1094]
2.  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 3.2.1.98 created 1978]
 
 
EC 3.2.1.99     
Accepted name: arabinan endo-1,5-α-L-arabinanase
Reaction: Endohydrolysis of (1→5)-α-arabinofuranosidic linkages in (1→5)-arabinans
Other name(s): endo-1,5-α-L-arabinanase; endo-α-1,5-arabanase; endo-arabanase; 1,5-α-L-arabinan 1,5-α-L-arabinanohydrolase; arabinan endo-1,5-α-L-arabinosidase (misleading)
Systematic name: 5-α-L-arabinan 5-α-L-arabinanohydrolase
Comments: Acts best on linear 1,5-α-L-arabinan. Also acts on branched arabinan, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 75432-96-1
References:
1.  Kaji, A. and Saheki, T. Endo-arabinanase from Bacillus subtilis F-11. Biochim. Biophys. Acta 410 (1975) 354–360. [DOI] [PMID: 1096]
2.  Weinstein, L. and Albersheim, P. Structure of plant cell walls. IX. Purification and partial characterization of a wall-degrading endo-arabinase and an arabinosidase from Bacillus subtilis. Plant Physiol. 63 (1979) 425–432. [PMID: 16660741]
3.  Flipphi, M.J., Panneman, H., van der Veen, P., Visser, J. and de Graaff, L.H. Molecular cloning, expression and structure of the endo-1,5-α-L-arabinase gene of Aspergillus niger. Appl. Microbiol. Biotechnol. 40 (1993) 318–326. [PMID: 7764386]
4.  Leal, T.F. and de Sa-Nogueira, I. Purification, characterization and functional analysis of an endo-arabinanase (AbnA) from Bacillus subtilis. FEMS Microbiol. Lett. 241 (2004) 41–48. [DOI] [PMID: 15556708]
[EC 3.2.1.99 created 1981, modified 2011]
 
 
EC 3.2.1.100     
Accepted name: mannan 1,4-mannobiosidase
Reaction: Hydrolysis of (1→4)-β-D-mannosidic linkages in (1→4)-β-D-mannans, to remove successive mannobiose residues from the non-reducing chain ends
Other name(s): 1,4-β-D-mannan mannobiohydrolase; exo-β-mannanase; exo-1,4-β-mannobiohydrolase
Systematic name: 4-β-D-mannan mannobiohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81811-49-6
References:
1.  Araki, T. and Kitamikado, M. Purification and characterization of a novel exo-β-mannanase from Aeromonas sp. F-25. J. Biochem. (Tokyo) 91 (1982) 1181–1186. [PMID: 7096283]
[EC 3.2.1.100 created 1983]
 
 


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