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, PDB, 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] |
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|
|
|
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; NAHase |
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])] |
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|
|
|
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, PDB, CAS registry number: 9054-43-7 |
References: |
1. |
Frohwein, Y.S. and Gatt, S. Isolation of β-N-acetylhexosaminidase, β-N-acetylglucosaminidase, and β-N-acetylgalactosaminidase from calf brain. Biochemistry 6 (1967) 2775–2782. [PMID: 6055190] |
2. |
Hoogwinkel, G.J.M., Veltkamp, W.A., Overdijk, B. and Lisman, J.W. Electrophoretic separation of β-N-acetylhexosaminidases of human and bovine brain and liver and of Tay-Sachs brain tissue. Hoppe-Seylers Z. Physiol. Chem. 353 (1972) 839–841. [PMID: 5069351] |
|
[EC 3.2.1.53 created 1972] |
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|
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, PDB, 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)] |
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|
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|
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] |
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|
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|
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] |
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[EC 3.2.1.56 created 1972] |
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|
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] |
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|
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] |
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|
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, PDB, 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] |
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|
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] |
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|
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] |
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|
EC |
3.2.1.62 |
Accepted name: |
glycosylceramidase |
Reaction: |
(1) a β-D-glucosyl-N-acylsphingosine + H2O = a ceramide + β-D-glucose (2) a β-D-galactosyl-N-acylsphingosine + H2O = a ceramide + β-D-galactose (3) a flavonoid-O-β-D-glucoside + H2O = a flavonoid + β-D-glucose |
|
For diagram of phloretin biosynthesis, click here and 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; LPH (gene name); LCT (gene name); glycosyl-N-acylsphingosine glycohydrolase |
Systematic name: |
β-D-glucosyl-N-acylsphingosine glycohydrolase (configuration-retaining) |
Comments: |
The enzyme, found in the intestinal mucosa, hydrolyses β-D-glucosyl and β-D-galactosyl residues from a very broad range of substrates using a retaining mechanism. Characterized substrates include glucosyl- and galactosyl-ceramides [3], O3-, O4′ and O7-glucosylated flavonoids [6], and the 2′-O-glucosylated dihydrochalcone phlorizin [1]. The enzyme includes two glycosyl hydrolase domains, both belonging to the GH1 family. While one domain is responsible for the activity described here, the other catalyses the reaction of EC 3.2.1.108, lactase [4,5]. cf. EC 3.2.1.45, glucosylceramidase and EC 3.2.1.46, galactosylceramidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-10-7 |
References: |
1. |
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] |
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. |
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. [DOI] [PMID: 4752949] |
4. |
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. [DOI] [PMID: 9762914] |
5. |
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. [DOI] [PMID: 11106409] |
6. |
Nemeth, K., Plumb, G.W., Berrin, J.G., Juge, N., Jacob, R., Naim, H.Y., Williamson, G., Swallow, D.M. and Kroon, P.A. Deglycosylation by small intestinal epithelial cell β-glucosidases is a critical step in the absorption and metabolism of dietary flavonoid glycosides in humans. Eur J Nutr 42 (2003) 29–42. [DOI] [PMID: 12594539] |
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[EC 3.2.1.62 created 1972, modified 1976, modified 2022] |
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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, PDB, 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] |
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[EC 3.2.1.63 created 1972] |
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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] |
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[EC 3.2.1.64 created 1972, modified 2004] |
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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] |
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|
EC
|
3.2.1.66
|
Deleted entry: | The activity is covered by EC 3.2.1.40, α-L-rhamnosidase |
[EC 3.2.1.66 created 1972, deleted 2021] |
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|
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, PDB, 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] |
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|
|
|
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] |
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|
|
|
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, PDB, CAS registry number: 37288-49-6 |
References: |
1. |
Reese, E.T., Parrish, F.W. and Mandels, M. β-D-1,2-Glucanases in fungi. Can. J. Microbiol. 7 (1961) 309–317. [PMID: 13740314] |
|
[EC 3.2.1.71 created 1972] |
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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] |
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|
|
|
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] |
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|
|
|
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, PDB, 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] |
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|
|
|
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, PDB, 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] |
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|
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|
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] |
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|
|
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] |
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|
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] |
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|
|
|
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] |
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|
|
|
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] |
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|
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, PDB, 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] |
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|
|
|
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] |
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[EC 3.2.1.82 created 1972, modified 2019] |
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|
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] |
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|
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|
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, PDB, 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] |
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|
|
|
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] |
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|
|
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] |
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|
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] |
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|
|
|
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] |
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|
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|
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] |
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|
|
|
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] |
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|
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] |
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|
|
|
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, PDB, 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] |
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|
|
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] |
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|
|
|
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] |
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|
|
|
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. [DOI] [PMID: 1027432] |
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] |
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|
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] |
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|
|
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, PDB, 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] |
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|
|
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] |
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[EC 3.2.1.100 created 1983] |
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