2)-L-fucosidaseSee separate files for EC 3.2.1.101 to EC 3.2.1.150 and EC 3.2.1.151 to EC 3.2.1.180.
See the following file for:
EC 3.2.1.101 to EC 3.2.1.150
EC 3.2.1.151 to EC 3.2.1.180
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, 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.
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]
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, 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]
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, 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]
Accepted name: cyclomaltodextrinase
Reaction: cyclomaltodextrin + H2O = linear maltodextrin
Other name(s): cycloheptaglucanase; cyclohexaglucanase; cyclodextrinase
Systematic name: cyclomaltodextrin dextrin-hydrolase (decyclizing)
Comments: Also hydrolyses linear maltodextrin.
Links to other databases: BRENDA, EXPASY, KEGG, 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]
Accepted name: α-N-arabinofuranosidase
Reaction: Hydrolysis of terminal non-reducing α-L-arabinofuranoside residues in α-L-arabinosides
Other name(s): arabinosidase; α-arabinosidase; α-L-arabinosidase; α-arabinofuranosidase;polysaccharide α-L-arabinofuranosidase; α-L-arabinofuranoside hydrolase; L-arabinosidase; α-L-arabinanase
Systematic name: α-L-arabinofuranoside arabinofuranohydrolase
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.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9067-74-7
References:
1. 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]
2. Kaji, A. and Yoshihara, O. Properties of purified α-L-arabinofuranosidase from Corticium rolfsii. Biochim. Biophys. Acta 250 (1971) 367-371. [PMID: 5143344]
3. 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.
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, 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]
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, 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.
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, 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]
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, 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]
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, 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]
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, 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]
Accepted name: glycosylceramidase
Reaction: a glycosyl-N-acylsphingosine + H2O = an N-acylsphingosine + a sugar
For diagram of the reaction 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, 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]
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-(12)-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, 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]
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, 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]
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, CAS registry number: 9041-11-6
References:
1. Avigad, G. and Bauer, S. Fructan hydrolases. Methods Enzymol. 8 (1966) 621-628.
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, CAS registry number: 37288-47-4
References:
1. Westlake, D.W.S. Microbiological degradation of quercitrin. Can. J. Microbiol. 9 (1963) 211-220.
Accepted name: galacturan 1,4-α-galacturonidase
Reaction: [(1→4)-α-D-galacturonide]n + H2O = [(1→4)-α-D-galacturonide]n-1 + D-galacturonate
Other name(s): exopolygalacturonase; poly(galacturonate) hydrolase; exo-D-galacturonase; exo-D-galacturonanase; exopoly-D-galacturonase; poly(1,4-α-D-galacturonide) galacturonohydrolase
Systematic name: poly[(1→4)-α-D-galacturonide] galacturonohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, 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]
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, 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 3.2.1.69 Deleted entry: amylopectin 6-glucanohydrolase. Now included with EC 3.2.1.41 pullulanase (EC 3.2.1.69 created 1972, deleted 1976)]
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, 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]
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, 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.
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, 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.
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, 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.
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, 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.
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, 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.
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, 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.
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, 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]
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, 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 3.2.1.79 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)]
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, 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]
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 polysaccharide
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, 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]
Accepted name: exo-poly-α-galacturonosidase
Reaction: Hydrolysis of pectic acid from the non-reducing end, releasing digalacturonate
Other name(s): exopolygalacturonosidase; exopolygalacturanosidase; poly(1,4-α-D-galactosiduronate) digalacturonohydrolase
Systematic name: poly[(1→4)-α-D-galactosiduronate] digalacturonohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, 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.
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, 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]
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, 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]
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, 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]
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, 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]
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, 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]
Accepted name: β-L-arabinosidase
Reaction: a β-L-arabinoside + H2O = L-arabinose + an alcohol
Other name(s): vicianosidase
Systematic name: β-L-arabinoside arabinohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, 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]
Accepted name: arabinogalactan endo-1,4-β-galactosidase
Reaction: Endohydrolysis of (1→4)-β-D-galactosidic linkages in arabinogalactans
Other name(s): endo-1,4-β-galactanase; galactanase; arabinogalactanase
Systematic name: arabinogalactan 4-β-D-galactanohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, 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]
[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)]
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, 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]
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, 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]
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, 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]
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, 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.
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, 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]
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-(14)-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, 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]
Accepted name: endo-α-N-acetylgalactosaminidase
Reaction: 3-O-β-D-galactosyl-N-acetyl-α-D-galactosaminyl-L-serine-[protein] + H2O = 3-O-β-D-galactosyl-N-acetyl-α-D-galactosamine + L-serine-[protein]
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 Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1→3)-β-GalNAc. The enzymes from Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. release of 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, 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]
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, 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.
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, 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]
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, 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]