Enzyme Nomenclature

EC 3.2.1 (continued)

Hydrolysing O-Glycosyl Compounds

Continued from EC 3.2.1.1 to EC 3.2.1.50

See separate files for EC 3.2.1.101 to EC 3.2.1.150 and EC 3.2.1.151 to EC 3.2.1.209.

Contents

EC 3.2.1.51 α-L-fucosidase
EC 3.2.1.52 β-L-N-acetylhexosaminidase
EC 3.2.1.53 β-N-acetylgalactosaminidase
EC 3.2.1.54 cyclomaltodextrinase
EC 3.2.1.55 non-reducing end α-L-arabinofuranosidase
EC 3.2.1.56 glucuronosyl-disulfoglucosamine glucuronidase
EC 3.2.1.57 isopullulanase
EC 3.2.1.58 glucan 1,3-β-glucosidase
EC 3.2.1.59 glucan endo-1,3-α-glucosidase
EC 3.2.1.60 glucan 1,4-α-maltotetraohydrolase
EC 3.2.1.61 mycodextranase
EC 3.2.1.62 glycosylceramidase
EC 3.2.1.63 1,2-α-L-fucosidase
EC 3.2.1.64 2,6-β-fructan 6-levanbiohydrolase
EC 3.2.1.65 levanase
EC 3.2.1.66 quercitrinase
EC 3.2.1.67 galacturan 1,4-α-galacturonidase
EC 3.2.1.68 isoamylase
EC 3.2.1.69 deleted, included in EC 3.2.1.41
EC 3.2.1.70 glucan 1,6-α-glucosidase
EC 3.2.1.71 glucan endo-1,2-β-glucosidase
EC 3.2.1.72 xylan 1,3-β-xylosidase
EC 3.2.1.73 licheninase
EC 3.2.1.74 glucan 1,4-β-glucosidase
EC 3.2.1.75 glucan endo-1,6-β-glucosidase
EC 3.2.1.76 L-iduronidase
EC 3.2.1.77 mannan 1,2-(1,3)-α-mannosidase
EC 3.2.1.78 mannan endo-1,4-β-mannosidase
EC 3.2.1.79 deleted, included in EC 3.2.1.55
EC 3.2.1.80 fructan β-fructosidase
EC 3.2.1.81 β-agarase
EC 3.2.1.82 exo-poly-α-galacturonosidase
EC 3.2.1.83 κ-carrageenase
EC 3.2.1.84 glucan 1,3-α-glucosidase
EC 3.2.1.85 6-phospho-β-galactosidase
EC 3.2.1.86 6-phospho-β-glucosidase
EC 3.2.1.87 capsular-polysaccharide endo-1,3-α-galactosidase
EC 3.2.1.88 non-reducing end β-L-arabinopyranosidase
EC 3.2.1.89 arabinogalactan endo-β-1,4-galactanase
EC 3.2.1.90 deleted, not sufficiently characterised
EC 3.2.1.91 cellulose 1,4-β-cellobiosidase (non-reducing end)
EC 3.2.1.92 peptidoglycan β-N-acetylmuramidase
EC 3.2.1.93 α,α-phosphotrehalase
EC 3.2.1.94 glucan 1,6-α-isomaltosidase
EC 3.2.1.95 dextran 1,6-α-isomaltotriosidase
EC 3.2.1.96 mannosyl-glycoprotein endo-β-N-acetylglucosaminidase
EC 3.2.1.97 endo-α-N-acetylgalactosaminidase
EC 3.2.1.98 glucan 1,4-α-maltohexaosidase
EC 3.2.1.99 arabinan endo-1,5-α-L-arabinanase
EC 3.2.1.100 mannan 1,4-mannobiosidase

See the following file for:

EC 3.2.1.101 to EC 3.2.1.150
EC 3.2.1.151 to EC 3.2.1.209

Entries

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.

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. [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. [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-beta-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, 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)]

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. [PMID: 5452669]

3. Kaji, A. and Yoshihara, O. Properties of purified α-L-arabinofuranosidase from Corticium rolfsii. Biochim. Biophys. Acta 250 (1971) 367-371. [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. [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

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, 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. [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. [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[(1→3);(1→4)]-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. [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. [PMID: 5652425]

[EC 3.2.1.61 created 1972]

EC 3.2.1.62

Accepted name: glycosylceramidase

Reaction: a glycosyl-N-acylsphingosine + H2O = an N-acylsphingosine + a sugar

For diagram of the reaction click here or click here.

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. [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. [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. [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. [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. [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. [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. [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

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, ExplorEnz, 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. [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. [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. [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.

[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

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.

[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. [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. [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.

[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. [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, 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. [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. [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. [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. [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, ExplorEnz, 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. [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, 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. [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. [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. [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. [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. [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. [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. [PMID: 17056685]

[EC 3.2.1.89 created 1976, modified 2012]

[EC 3.2.1.90 Deleted entry: arabinogalactan endo-1,3-β-galactosidase not sufficiently characterised. (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. [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. [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. [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. [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 names: 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

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. [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. [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. [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. [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. [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. [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. [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. [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, 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. [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. [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]


Continued with EC 3.2.1.101 to EC 3.2.1.150
Return to EC 3 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page