Continued from EC 3.1.21 to EC 3.1.31
EC 3.2.1 Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds
EC 3.2.2 Hydrolysing N-Glycosyl Compounds
EC 3.2.3 Hydrolysing S-Glycosyl Compounds (discontinued)
EC 3.2.1.1 α-amylase
EC 3.2.1.2 β-amylase
EC 3.2.1.3 glucan 1,4-α-glucosidase
EC 3.2.1.4 cellulase
EC 3.2.1.5 deleted
EC 3.2.1.6 endo-1,3(4)-β-glucanase
EC 3.2.1.7 inulinase
EC 3.2.1.8 endo-1,4-β-xylanase
EC 3.2.1.9 deleted
EC 3.2.1.10 oligo-1,6-glucosidase
EC 3.2.1.11 dextranase
EC 3.2.1.12 deleted, included in EC 3.2.1.54
EC 3.2.1.13 deleted, included in EC 3.2.1.54
EC 3.2.1.14 chitinase
EC 3.2.1.15 endo-polygalacturonase
EC 3.2.1.16 deleted
EC 3.2.1.17 lysozyme
EC 3.2.1.18 exo-α-sialidase
EC 3.2.1.19 deleted
EC 3.2.1.20 α-glucosidase
EC 3.2.1.21 β-glucosidase
EC 3.2.1.22 α-galactosidase
EC 3.2.1.23 β-galactosidase
EC 3.2.1.24 α-mannosidase
EC 3.2.1.25 β-mannosidase
EC 3.2.1.26 β-fructofuranosidase
EC 3.2.1.27 deleted
EC 3.2.1.28 α,α-trehalase
EC 3.2.1.29 deleted, included in EC 3.2.1.52
EC 3.2.1.30 deleted, included in EC 3.2.1.52
EC 3.2.1.31 β-glucuronidase
EC 3.2.1.32 endo-1,3-β-xylanase
EC 3.2.1.33 amylo-1,6-glucosidase
EC 3.2.1.34 deleted, included in EC 3.2.1.35
EC 3.2.1.35 hyaluronoglucosaminidase
EC 3.2.1.36 hyaluronoglucuronidase
EC 3.2.1.37 xylan 1,4-β-xylosidase
EC 3.2.1.38 β-D-fucosidase
EC 3.2.1.39 glucan endo-1,3-β-D-glucosidase
EC 3.2.1.40 α-L-rhamnosidase
EC 3.2.1.41 pullulanase
EC 3.2.1.42 GDP-glucosidase
EC 3.2.1.43 β-L-rhamnosidase
EC 3.2.1.44 now EC 3.2.1.211 and EC 3.2.1.212
EC 3.2.1.45 glucosylceramidase
EC 3.2.1.46 galactosylceramidase
EC 3.2.1.47 deleted covered by EC 3.2.1.22
EC 3.2.1.48 sucrose α-glucosidase
EC 3.2.1.49 α-N-acetylgalactosaminidase
EC 3.2.1.50 α-N-acetylglucosaminidase
See the following files for:
EC 3.2.1.51 to EC 3.2.1.100
EC 3.2.1.101 to EC 3.2.1.150
EC 3.2.1.151 to EC 3.2.1.227
Accepted name: α-amylase
Reaction: Endohydrolysis of (1→4)-α-D-glucosidic linkages in polysaccharides containing three or more (1→4)-α-linked D-glucose units
Other name(s): glycogenase; α-amylase; endoamylase; Taka-amylase A; 1,4-α-D-glucan glucanohydrolase
Systematic name: 4-α-D-glucan glucanohydrolase
Comments: Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the α-configuration. The term ‘α’ relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9000-90-2
References:
1. Fischer, E.H. and Stein, E.A. α-Amylases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 313-343.
2. Manners, D.J. Enzymic synthesis and degradation of starch and glycogen. Adv. Carbohydr. Chem. 17 (1962) 371-430.
3. Schwimmer, S. and Balls, A.K. Isolation and properties of crystalline α-amylase from germinated barley. J. Biol. Chem. 179 (1949) 1063-1074.
Accepted name: β-amylase
Reaction: Hydrolysis of (1→4)-α-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
Other name(s): saccharogen amylase; glycogenase; β-amylase; 1,4-α-D-glucan maltohydrolase
Systematic name: 4-α-D-glucan maltohydrolase
Comments: Acts on starch, glycogen and related polysaccharides and oligosaccharides producing β-maltose by an inversion. The term ‘β’ relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9000-91-3
References:
1. Balls, A.K., Walden, M.K. and Thompson, R.R. A crystalline β-amylase from sweet potatoes. J. Biol. Chem. 173 (1948) 9-19.
2. French, D. β-Amylases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 345-368.
3. Manners, D.J. Enzymic synthesis and degradation of starch and glycogen. Adv. Carbohydr. Chem. 17 (1962) 371-430.
Accepted name: glucan 1,4-α-glucosidase
Reaction: Hydrolysis of terminal (1→4)-linked α-D-glucose residues successively from non-reducing ends of the chains with release of β-D-glucose
Other name(s): glucoamylase; amyloglucosidase; γ-amylase; lysosomal α-glucosidase; acid maltase; exo-1,4-α-glucosidase; glucose amylase; γ-1,4-glucan glucohydrolase; acid maltase; 1,4-α-D-glucan glucohydrolase
Systematic name: 4-α-D-glucan glucohydrolase
Comments: Most forms of the enzyme can rapidly hydrolyse 1,6-α-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyse 1,6- and 1,3-α-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 α-glucosidase, from mammalian intestine, can catalyse similar reactions.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9032-08-0
References:
1. French, D. and Knapp, D.W. The maltase of Clostridium acetobutylicum. J. Biol. Chem. 187 (1950) 463-471.
2. Illingworth Brown, B. and Brown, D.H. The subcellular distribution of enzymes in type II glycogenosis and the occurrence of an oligo-α-1,4-glucan glucohydrolase in human tissues. Biochim. Biophys. Acta 110 (1965) 124-133. [PMID: 4286143]
3. Jeffrey, P.L., Brown, D.H. and Brown, B.I. Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme. Biochemistry 9 (1970) 1403-1415. [PMID: 4313883]
4. Kelly, J.J. and Alpers, D.H. Properties of human intestinal glucoamylase. Biochim. Biophys. Acta 315 (1973) 113-122. [PMID: 4743896]
5. Miller, K.D. and Copeland, W.H. A blood trans-α-glucosylase. Biochim. Biophys. Acta 22 (1956) 193-194.
6. Tsujisaka, Y., Fukimoto, J. and Yamamoto, T. Specificity of crystalline saccharogenic amylase of moulds. Nature 181 (1958) 770-771.
Accepted name: cellulase
Reaction: Endohydrolysis of (1→4)-β-D-glucosidic linkages in cellulose, lichenin and cereal β-D-glucans
Other name(s): endo-1,4-β-D-glucanase; β-1,4-glucanase; β-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS; 1,4-(1,3;1,4)-β-D-glucan 4-glucanohydrolase
Systematic name: 4-(1,3;1,4)-β-D-glucan 4-glucanohydrolase
Comments: Will also hydrolyse 1,4-linkages in β-D-glucans also containing 1,3-linkages.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9012-54-8
References:
1. Datta, P.K., Hanson, K.R. and Whitaker, D.R. Improved procedures for preparation and characterization of Myrothecum cellulase. III. Molecular weight, amino acid composition, terminal residues, and other properties. Can. J. Biochem. Physiol. 41 (1963) 697-705. [PMID: 14025219]
2. Larner, J. Other glucosidases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 369-378.
3. Myers, F.L. and Northcote, D.H. Partial purification and some properties of a cellulase from Helix pomatia. Biochem. J. 71 (1959) 749-756.
4. Nishizawa, K. and Hashimoto, Y. Cellulose splitting enzymes. VI. Difference in the specificities of cellulase and β-glucosidase from Irpex lacteus. Arch. Biochem. Biophys. 81 (1959) 211-222.
5. Whitaker, D.R., Hanson, K.R. and Datta, P.K. Improved procedures for preparation and characterization of myrothecium cellulase. 2. Purification procedures. Can. J. Biochem. Physiol. 41 (1963) 671-696.
6. Hatfield, R. and Nevins, D.J. Purification and properties of an endoglucanase isolated from the cell walls of Zea mays seedlings. Carbohydr. Res. 148 (1986) 265-278.
7. Hatfield, R. and Nevins, D.J. Hydrolytic activity and substrate specificity of an endoglucanase from Zea mays seedling cell walls. Plant Physiol. 83 (1987) 203-207.
8. Inohue, M., Hayashgi, K. and Nevins, D.J. Polypeptide characteristics and immunological properties of exo- and endoglucanases purified from maize coleoptile cell walls. J. Plant Physiol. 154 (1999) 334-340.
[EC 3.2.1.5 Deleted entry: licheninase (EC 3.2.1.5 created 1961, deleted 1964)]
Accepted name: endo-1,3(4)-β-glucanase
Reaction: Endohydrolysis of (1→3)- or (1→4)-linkages in β-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3
Other name(s): endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3(4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1→3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-β-(1-3)-D-glucanase; endo-β-1,3-glucanase IV; endo-1,3-β-D-glucanase; 1,3-(1,3;1,4)-β-D-glucan 3(4)-glucanohydrolase
Systematic name: 3-(1→3;1→4)-β-D-glucan 3(4)-glucanohydrolase
Comments: Substrates include laminarin, lichenin and cereal D-glucans; different from EC 3.2.1.52 β-N-acetylhexosaminidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 62213-14-3
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]
3. Cunningham, L.W. and Manners, D.J. Enzymic degradation of lichenin. Biochem. J. 80 (1961) 42P-43P.
4. Reese, E.T. and Mandels, M. β-D-1,3-Glucanases in fungi. Can. J. Microbiol. 5 (1959) 173-185.
5. Sova, V.V., Elyakova, L.A. and Vaskovsky, V.E. Purification and some properties of β-1,3-glucan glucanohydrolase from the crystalline style of bivalvia, Spisula sachalinensis. Biochim. Biophys. Acta 212 (1970) 111-115. [PMID: 5500926]
Accepted name: inulinase
Reaction: Endohydrolysis of (2→1)-β-D-fructosidic linkages in inulin
Other name(s): inulase; indoinulinase; endo-inulinase; exoinulinase; 2,1-β-D-fructan fructanohydrolase
Systematic name: 1-β-D-fructan fructanohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-67-6
References:
1. Adams, M., Richtmyer, N.K. and Hudson, C.S. Some enzymes present in highly purified invertase preparations; a contribution to the study of fructofuranosidases, galactosidases, glucosidases and mannosidases. J. Am. Chem. Soc. 65 (1943) 1369-1380.
Accepted name: endo-1,4-β-xylanase
Reaction: Endohydrolysis of (1→4)-β-D-xylosidic linkages in xylans
Other name(s): endo-(1→4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase
Systematic name: 4-β-D-xylan xylanohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-57-4
References:
1. Howard, B.H., Jones, G. and Purdom, M.R. The pentosanases of some rumen bacteria. Biochem. J. 74 (1960) 173-180.
2. Whistler, R.L. and Masek, E. Enzymatic hydolysis of xylan. J. Am. Chem. Soc. 77 (1955) 1241-1243.
[EC 3.2.1.9 Deleted entry: amylopectin-1,6-glucosidase (EC 3.2.1.9 created 1961, deleted 1972)]
Accepted name: oligo-1,6-glucosidase
Reaction: Hydrolysis of (1→6)-α-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (α-amylase), and in isomaltose
Other name(s): limit dextrinase (erroneous); isomaltase; sucrase-isomaltase; exo-oligo-1,6-glucosidase; dextrin 6α-glucanohydrolase; α-limit dextrinase; dextrin 6-glucanohydrolase; oligosaccharide α-1,6-glucohydrolase; α-methylglucosidase
Systematic name: oligosaccharide α-1,6-glucohydrolase
Comments: This enzyme, like EC 3.2.1.33 (amylo-α-1,6-glucosidase), can release an α-1→6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41 (pullulanase), EC 3.2.1.142 (limit dextrinase), and EC 3.2.1.68 (isoamylase) is maltose. It also hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. The enzyme from intestinal mucosa is a single polypeptide chain that also catalyses the reaction of EC 3.2.1.48 (sucrose α-glucosidase). Differs from EC 3.2.1.33 (amylo-α-1,6-glucosidase) in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9032-15-9
References:
1. Hauri, H.-P., Quaroni, A. and Isselbacher, K.J. Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase. Proc. Natl. Acad. Sci. USA 76 (1979) 5183-5186. [PMID: 291933]
2. Sjöström, H., Norén, O., Christiansen, L., Wacker, H. and Semenza, G. A fully active, two-active-site, single-chain sucrase-isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein. J. Biol. Chem. 255 (1980) 11332-11338. [PMID: 7002920]
3. Rodriguez, I.R., Taravel, F.R. and Whelan, W.J. Characterization and function of pig intestinal sucrase-isomaltase and its separate subunits. Eur J Biochem. 143 (1984) 575-582. [PMID: 6479163]
Accepted name: dextranase
Reaction: Endohydrolysis of (1→6)-α-D-glucosidic linkages in dextran
Other name(s): dextran hydrolase; endodextranase; dextranase DL 2; DL 2; endo-dextranase; α-D-1,6-glucan-6-glucanohydrolase; 1,6-α-D-glucan 6-glucanohydrolase
Systematic name: 6-α-D-glucan 6-glucanohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-70-1
References:
1. Bailey, R.W. and Clarke, R.T.J. A bacterial dextranase. Biochem. J. 72 (1959) 49-54.
2. Deuel, H. and Stutz, E. Pectic substances and pectic enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 20 (1958) 341-382.
3. Fischer, E.H. and Stein, E.A. Cleavage of O- and S-glycosidic bonds (survey), in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York , 1960, pp. 301-312.
4. Rozenfel'd, E.L. and Lukomskaya, I.S. [The hydrolysis of 1:6 bonds of dextran by animal tissues.] Biokhimiya 21 (1956) 412-415. (in Russian)
[EC 3.2.1.12 Deleted entry: cycloheptaglucanase. Now included with EC 3.2.1.54 cyclomaltodextrinase (EC 3.2.1.12 created 1961, deleted 1976)]
[EC 3.2.1.13 Deleted entry: cyclohexaglucanase. Now included with EC 3.2.1.54 cyclomaltodextrinase (EC 3.2.1.13 created 1961, deleted 1976)]
Accepted name: chitinase
Reaction: Random endo-hydrolysis of N-acetyl-β-D-glucosaminide (1→4)-β-linkages in chitin and chitodextrins
Glossary: chitin = [(1→4)-β-D-GlcpNAc]n = (1→4)-2-acetamido-2-deoxy-β-D-glucan
Other name(s): ChiC; chitodextrinase (ambiguous); 1,4-β-poly-N-acetylglucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase
Systematic name: (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase
Comments: The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo-chitodextrinases can act. Activity is greatly stimulated in the presence of EC 1.14.99.53, lytic chitin monoxygenase, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase. cf. EC 3.2.1.202, endo-chitodextrinase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-06-3
References:
1. Zechmeister, L. and Tóth, G. Chromatographic adsorption of the enzymes of emulsin which act on chitins. Enzymologia 7 (1939) 165-169.
2. Tracey, M.V. Chitinase in some basidiomycetes. Biochem. J. 61 (1955) 579-586. [PMID: 13276340]
3. Fischer, E.H. and Stein, E.A. Cleavage of O- and S-glycosidic bonds (survey). In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 301-312.
4. Connell, T.D., Metzger, D.J., Lynch, J. and Folster, J.P. Endochitinase is transported to the extracellular milieu by the eps-encoded general secretory pathway of Vibrio cholerae. J. Bacteriol. 180 (1998) 5591-5600. [PMID: 9791107]
5. Francetic, O., Badaut, C., Rimsky, S. and Pugsley, A.P. The ChiA (YheB) protein of Escherichia coli K-12 is an endochitinase whose gene is negatively controlled by the nucleoid-structuring protein H-NS. Mol. Microbiol. 35 (2000) 1506-1517. [PMID: 10760150]
6. Zverlov, V.V., Fuchs, K.P. and Schwarz, W.H. Chi18A, the endochitinase in the cellulosome of the thermophilic, cellulolytic bacterium Clostridium thermocellum. Appl. Environ. Microbiol. 68 (2002) 3176-3179. [PMID: 12039789]
7. Rottloff, S., Stieber, R., Maischak, H., Turini, F.G., Heubl, G. and Mithofer, A. Functional characterization of a class III acid endochitinase from the traps of the carnivorous pitcher plant genus, Nepenthes. J. Exp. Bot. 62 (2011) 4639-4647. [PMID: 21633084]
Accepted name: endo-polygalacturonase
Reaction: (1,4-α-D-galacturonosyl)n+m + H2O = (1,4-α-D-galacturonosyl)n + (1,4-α-D-galacturonosyl)m
Other name(s): pectin depolymerase (ambiguous); pectinase (ambiguous); endopolygalacturonase; pectolase (ambiguous); pectin hydrolase (ambiguous); pectin polygalacturonase (ambiguous); polygalacturonase (ambiguous); poly-α-1,4-galacturonide glycanohydrolase (ambiguous); endogalacturonase; endo-D-galacturonase; poly(1,4-α-D-galacturonide) glycanohydrolase (ambiguous)
Systematic name: (1→4)-α-D-galacturonan glycanohydrolase (endo-cleaving)
Comments: The enzyme catalyses the random hydrolysis of (1→4)-α-D-galactosiduronic linkages in pectate and other galacturonans. Different forms of the enzyme have different tolerances to methyl esterification of the substrate.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, PDB, CAS registry number: 9032-75-1
References:
1. Lineweaver, H. and Jansen, E.F. Pectic enzymes. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 267-295.
2. McCready, R.M. and Seegmiller, C.G. Action of pectic enzymes on oligogalacturonic acids and some of their derivatives. Arch. Biochem. Biophys. 50 (1954) 440-450. [PMID: 13159344]
3. Phaff, H.J. and Demain, A.L. The unienzymatic nature of yeast polygalacturonase. J. Biol. Chem. 218 (1956) 875-884. [PMID: 13295238]
4. Deuel, H. and Stutz, E. Pectic substances and pectic enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 20 (1958) 341-382. [PMID: 13605988]
5. Mill, P.J. and Tuttobello, R. The pectic enzymes of Aspergillus niger. 2. Endopolygalacturonase. Biochem. J. 79 (1961) 57-64. [PMID: 13770689]
[EC 3.2.1.16 Deleted entry: alginase (EC 3.2.1.16 created 1961, deleted 1972)]
Accepted name: lysozyme
Reaction: Hydrolysis of (1→4)-β-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Other name(s): muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme
Systematic name: peptidoglycan N-acetylmuramoylhydrolase
Comments: cf. also EC 3.2.1.14 chitinase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9001-63-2
References:
1. Blade, C.C.F., Johnson, L.N., Mair, G.A., North, A.C.T., Phillips, D.C. and Sarma, V.R. Crystallographic studies of the activity of hen egg-white lysozyme. Proc. R. Soc. Lond. B: Biol. Sci. 167 (1967) 378-388. [PMID: 4382801]
2. Blake, C.C.F., Mair, G.A., North, A.C.T., Phillips, D.C. and Sarma, V.R. On the conformation of the hen egg-white lysozyme molecule. Proc. R. Soc. Lond. B: Biol. Sci. 167 (1967) 365-377. [PMID: 4382800]
3. Jollès, P. Lysozyme, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 431-445.
Accepted name: exo-α-sialidase
Reaction: Hydrolysis of α-(2→3)-, α-(2→6)-, α-(2→8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates
Other name(s): neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase
Systematic name: acetylneuraminyl hydrolase
Comments: The enzyme does not act on 4-O-acetylated sialic acids. endo-α-Sialidase activity is listed as EC 3.2.1.129, endo-α-sialidase. See also EC 4.2.2.15 anhydrosialidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9001-67-6
References:
1. Schauer, R. Sialic acids. Adv. Carbohydr. Chem. Biochem. 40 (1982) 131-234.
2. Cabezas, J.A. Some questions and suggestions on the type references of the official nomenclature (IUB) for sialidase(s) and endosialidase. Biochem. J. 278 (1991) 311-312. [PMID: 1883340]
[EC 3.2.1.19 Deleted entry: heparinase (EC 3.2.1.19 created 1961, deleted 1978)]
Accepted name: α-glucosidase
Reaction: Hydrolysis of terminal, non-reducing (1→4)-linked α-D-glucose residues with release of α-D-glucose
Other name(s): maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; α-glucopyranosidase; glucosidoinvertase; α-D-glucosidase; α-glucoside hydrolase; α-1,4-glucosidase
Systematic name: α-D-glucoside glucohydrolase
Comments: This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of 1,4-α-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-α-glucosidase and, more slowly, hydrolyses 1,6-α-D-glucose links.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-42-7
References:
1. Bruni, C.B., Sica, V., Auricchio, F. and Covelli, I. Further kinetic and structural characterization of the lysosomal α-D-glucoside glucohydrolase from cattle liver. Biochim. Biophys. Acta 212 (1970) 470-477. [PMID: 5466143]
2. Flanagan, P.R. and Forstner, G.G. Purification of rat intestinal maltase/glucoamylase and its anomalous dissociation either by heat or by low pH. Biochem. J. 173 (1978) 553-563. [PMID: 29602]
3. Larner, J. Other glucosidases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York , 1960, pp. 369-378.
4. Sivikami, S. and Radhakrishnan, A.N. Purification of rabbit intestinal glucoamylase by affinity chromatography on Sephadex G-200. Indian J. Biochem. Biophys. 10 (1973) 283-284. [PMID: 4792946]
5. Sørensen, S.H., Norén, O., Sjöström, H. and Danielsen, E.M. Amphiphilic pig intestinal microvillus maltase/glucoamylase. Structure and specificity. Eur. J. Biochem. 126 (1982) 559-568. [PMID: 6814909]
Accepted name: β-glucosidase
Reaction: Hydrolysis of terminal, non-reducing β-D-glucosyl residues with release of β-D-glucose
Other name(s): gentiobiase; cellobiase; emulsin; elaterase; aryl-β-glucosidase; β-D-glucosidase; β-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl β-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; β-1,6-glucosidase
Systematic name: β-D-glucoside glucohydrolase
Comments: Wide specificity for β-D-glucosides. Some examples also hydrolyse one or more of the following: β-D-galactosides, α-L-arabinosides, β-D-xylosides, β-D-fucosides.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-22-3
References:
1. Chinchetru, M.A., Cabezas, J.A. and Calvo, P. Purification and characterization of a broad specificity β-glucosidase from sheep liver. Int. J. Biochem. 21 (1989) 469-476. [PMID: 2503402]
2. Conchie, J. β-Glucosidase from rumen liquor. Preparation, assay and kinetics of action. Biochem. J. 58 (1954) 552-560.
3. Dahlqvist, A. Pig intestinal β-glucosidase activities. I. Relation to β-galactosidase (lactase). Biochim. Biophys. Acta 50 (1961) 55-61.
4. Heyworth, R. and Walker, P.G. Almond-emulsin β-D-glucosidase and β-D-galactosidase. Biochem. J. 83 (1962) 331-335.
5. Larner, J. Other glucosidases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York , 1960, pp. 369-378.
6. Sano, K., Amemura, A. and Harada, T. Purification and properties of a β-1,6-glucosidase from Flavobacterium. Biochim. Biophys. Acta 377 (1975) 410-420. [PMID: 235305]
Accepted name: α-galactosidase
Reaction: Hydrolysis of terminal, non-reducing α-D-galactose residues in α-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids
Other name(s): melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase
Systematic name: α-D-galactoside galactohydrolase
Comments: Also hydrolyses α-D-fucosides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-35-8
References:
1. Suzuki, H., Li, S.-C. and Li, Y.-T. α-Galactosidase from Mortierella vinacea. Crystallization and properties. J. Biol. Chem. 245 (1970) 781-786. [PMID: 5418105]
2. Wiederschain, G. and Beyer, E. [Interrelation of α-D-fucosidase and α-D-galactosidase activities in man and animals]. Dokl. Akad. Nauk S.S.S.R. 231 (1976) 486-488. [PMID: 976079]
Accepted name: β-galactosidase
Reaction: Hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides
Other name(s): lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat
Systematic name: β-D-galactoside galactohydrolase
Comments: Some enzymes in this group hydrolyse α-L-arabinosides; some animal enzymes also hydrolyse β-D-fucosides and β-D-glucosides; cf. EC 3.2.1.108 lactase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9031-11-2
References:
1. Blakely, J.A. and MacKenzie, S.L. Purification and properties of a β-hexosidase from Sporobolomyces singularis. Can. J. Biochem. 47 (1969) 1021-1025. [PMID: 5389663]
2. Kuby, S.A. and Lardy, H.A. Purification and kinetics of β-D-galactosidase from Escherichia coli, strain K-12. J. Am. Chem. Soc. 75 (1953) 890-896.
3. Kuo, C.H. and Wells, W.W. β-Galactosidase from rat mammary gland. Its purification, properties, and role in the biosynthesis of 6β-O-D-galactopyranosyl myo-inositol. J. Biol. Chem. 253 (1978) 3550-3556. [PMID: 418065]
4. Landman, O.E. Properties and induction of β-galactosidase in Bacillus megaterium. Biochim. Biophys. Acta 23 (1957) 558-569.
5. Llanillo, M., Perez, N. and Cabezas, J.A. β-Galactosidase and β-glucosidase activities of the same enzyme from rabbit liver. Int. J. Biochem. 8 (1977) 557-564.
6. Monod, J. and Cohn, M. La biosynthèse induite des enzymes (adaptation enzymatique). Adv. Enzymol. Relat. Subj. Biochem. 13 (1952) 67-119.
7. Wallenfels, K. and Malhotra, O.P. in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 409-430.
8. Asp, N.G., Dahlqvist, A. and Koldovský, O. Human small-intestinal β-galactosidases. Separation and characterization of one lactase and one hetero β-galactosidase. Biochem. J. 114 (1969) 351-359. [PMID: 5822067]
Accepted name: α-mannosidase
Reaction: Hydrolysis of terminal, non-reducing α-D-mannose residues in α-D-mannosides
Systematic name: α-D-mannoside mannohydrolase
Other name(s): α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranosidase; 1,2-α-mannosidase; 1,2-α-D-mannosidase; exo-α-mannosidase
Comments: Also hydrolyses α-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9025-42-7
References:
1. Li, Y.-T. Presence of α-D-mannosidic linkage in glycoproteins. Liberation of D-mannose from various glycoproteins by α-mannosidase isolated from jack bean meal. J. Biol. Chem. 241 (1966) 1010-1012.
2. Winchester, B. Role of α-D-mannosidases in the biosynthesis and catabolism of glycoproteins. Biochem. Soc. Trans. 12 (1984) 522-524. [PMID: 6428944]
Accepted name: β-mannosidase
Reaction: Hydrolysis of terminal, non-reducing β-D-mannose residues in β-D-mannosides
Other name(s): mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase
Systematic name: β-D-mannoside mannohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-43-8
References:
1. Adams, M., Richtmyer, N.K. and Hudson, C.S. Some enzymes present in highly purified invertase preparations; a contribution to the study of fructofuranosidases, galactosidases, glucosidases and mannosidases. J. Am. Chem. Soc. 65 (1943) 1369-1380.
2. Bartholomew, B.A. and Perry, A.L. The properties of synovial fluid β-mannosidase activity. Biochim. Biophys. Acta 315 (1973) 123-127. [PMID: 4743897]
3. Deuel, H., Lewuenberger, R. and Huber, G. Über den enzymatischen Abbau von Carubin, dem Galaktomannan aus Ceratonia siliqua L. Helv. Chim. Acta 33 (1950) 942-946.
4. Hylin, J.W. and Sawai, K. The enzymatic hydrolysis of Leucaena glauca galactomannan. Isolation of crystalline galactomannan depolymerase. J. Biol. Chem. 239 (1964) 990-992.
Accepted name: β-fructofuranosidase
Reaction: Hydrolysis of terminal non-reducing β-D-fructofuranoside residues in β-D-fructofuranosides
Other name(s): invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase
Systematic name: β-D-fructofuranoside fructohydrolase
Comments: Substrates include sucrose; also catalyses fructotransferase reactions.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-57-4
References:
1. Myrbäck, K. Invertases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 379-396.
2. Neumann, N.P. and Lampen, J.O. Purification and properties of yeast invertase. Biochemistry 6 (1967) 468-475. [PMID: 4963242]
[EC 3.2.1.27 Deleted entry: α-1,3-glucosidase (EC 3.2.1.27 created 1961, deleted 1972)]
Accepted name: α,α-trehalase
Reaction: α,α-trehalose + H2O = β-D-glucose + α-D-glucose
Other name(s): trehalase
Systematic name: α,α-trehalose glucohydrolase
Comments: The enzyme is an anomer-inverting glucosidase that catalyses the hydrolysis of the α-glucosidic O-linkage of α,α-trehalose, releasing initially equimolar amounts of α- and β-D-glucose. It is widely distributed in microorganisms, plants, invertebrates and vertebrates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-52-9
References:
1. Myrbäck, K. and Örtenblad, B. Trehalose und Hefe. II. Trehalasewirkung von Hefepräparaten. Biochem. Z. 291 (1937) 61-69.
2. Kalf, G.F. and Rieder, S.V. The preparation and properties of trehalase. J. Biol. Chem. 230 (1958) 691-698. [PMID: 13525386]
3. Hehre, E.J., Sawai, T., Brewer, C.F., Nakano, M. and Kanda, T. Trehalase: stereocomplementary hydrolytic and glucosyl transfer reactions with α- and β-D-glucosyl fluoride. Biochemistry 21 (1982) 3090-3097. [PMID: 7104311]
4. Mori, H., Lee, J.H., Okuyama, M., Nishimoto, M., Ohguchi, M., Kim, D., Kimura, A. and Chiba, S. Catalytic reaction mechanism based on α-secondary deuterium isotope effects in hydrolysis of trehalose by European honeybee trehalase. Biosci. Biotechnol. Biochem. 73 (2009) 2466-2473. [PMID: 19897915]
[EC 3.2.1.29 Deleted entry: chitobiase. Now included with EC 3.2.1.52 β-L-N-acetylhexosaminidase (EC 3.2.1.29 created 1961, deleted 1972)]
[EC 3.2.1.30 Deleted entry: β-D-acetylglucosaminidase. Now included with EC 3.2.1.52 β-L-N-acetylhexosaminidase (EC 3.2.1.30 created 1961, deleted 1992)]
Accepted name: β-glucuronidase
Reaction: a β-D-glucuronoside + H2O = D-glucuronate + an alcohol
Other name(s): β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase
Systematic name: β-D-glucuronoside glucuronosohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9001-45-0
References:
1. Diez, T. and Cabezas, J.A. Properties of two molecular forms of β-glucuronidase from the mollusc Littorina littorea L. Eur. J. Biochem. 93 (1978) 301-311.
2. Doyle, M.L., Katzman, P.A. and Doisy, E.A. Production and properties of bacterial β-glucuronidase. J. Biol. Chem. 217 (1955) 921-930.
3. Fishman, W.H. Beta-glucuronidase. Adv. Enzymol. Relat. Subj. Biochem. 16 (1955) 361-409.
4. Levvy, G.A. and Marsh, C.A. β-Glucuronidase, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 397-407.
5. Wakabayashi, M. and Fishman, W.H. The comparative ability of β-glucuronidase preparations (liver, Escherichia coli, Helix pomatia, and Patella vulgata) to hydrolyze certain steroid glucosiduronic acids. J. Biol. Chem. 236 (1961) 996-1001.
Accepted name: endo-1,3-β-xylanase
Reaction: Random endohydrolysis of (1→3)-β-D-glycosidic linkages in (1→3)-β-D-xylans
Other name(s): xylanase (ambiguous); endo-1,3-β-xylosidase (misleading); 1,3-β-xylanase; 1,3-xylanase; β-1,3-xylanase; endo-β-1,3-xylanase; 1,3-β-D-xylan xylanohydrolase; xylan endo-1,3-β-xylosidase
Systematic name: 3-β-D-xylan xylanohydrolase
Comments: This enzyme is found mostly in marine bacteria, which break down the β(1,3)-xylan found in the cell wall of some green and red algae. The enzyme produces mainly xylobiose, xylotriose and xylotetraose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-55-2
References:
1. Chen, W.P., Matsuo, M. and Tsuneo, Y. Purification and some properties of β-1,3-xylanase from Aspergillus terreus A-07. Agric. Biol. Chem. 50 (1986) 1183-1194.
2. Aoki, T., Araki, T. and Kitamikado, M. Purification and characterization of an endo-β-1,3-xylanase from Vibrio species. Nippon Suisan Gakkaishi 54 (1988) 277-281.
3. Araki, T., Tani, S., Maeda, K., Hashikawa, S., Nakagawa, H. and Morishita, T. Purification and characterization of β-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214. Biosci. Biotechnol. Biochem. 63 (1999) 2017-2019. [PMID: 10635569]
4. Araki, T., Inoue, N. and Morishita, T. Purification and characterization of β-1,3-xylanase from a marine bacterium, Alcaligenes sp. XY-234. J. Gen. Appl. Microbiol. 44 (1998) 269-274. [PMID: 12501421]
5. Okazaki, F., Shiraki, K., Tamaru, Y., Araki, T. and Takagi, M. The first thermodynamic characterization of β-1,3-xylanase from a marine bacterium. Protein J. 24 (2005) 413-421. [PMID: 16328734]
Accepted name: amylo-α-1,6-glucosidase
Reaction: Hydrolysis of (1→6)-α-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin
Other name(s): amylo-1,6-glucosidase; dextrin 6-α-D-glucosidase; amylopectin 1,6-glucosidase; dextrin-1,6-glucosidase; glycogen phosphorylase-limit dextrin α-1,6-glucohydrolase
Systematic name: glycogen phosphorylase-limit dextrin 6-α-glucohydrolase
Comments: This enzyme hydrolyses an unsubstituted glucose unit linked by an α(1→6) bond to an α(1→4) glucose chain. The enzyme activity found in mammals and yeast is in a polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25 (4-α-glucanotransferase), which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-α-glucosidase activity can then hydrolyse. Together, these two activities constitute the glycogen debranching system.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9012-47-9
References:
1. Brown, D.H. and Brown, B.I. Enzymes of glycogen debranching: Amylo-1,6-glucosidase (I) and oligo-1,4<→1,4-glucanotransferase (II). Methods Enzymol. 8 (1966) 515-524.
2. Lee, E.Y.C., Carter, J.H., Nielsen, L.D. and Fischer, E.H. Purification and properties of yeast amylo-1,6-glucosidase-oligo-1,4 leads to 1,4-glucantransferase. Biochemistry 9 (1970) 2347-2355. [PMID: 5424210]
3. Nelson, T.E., Kolb, E. and Larner, J. Purification and properties of rabbit muscle amylo-1,6-glucosidase-oligo-1,4-1,4-transferase. Biochemistry 8 (1969) 1419-1428. [PMID: 5805288]
[EC 3.2.1.34 Deleted entry: chondroitinase. Now included with EC 3.2.1.35 hyalurononglucosaminidase (EC 3.2.1.34 created 1965, deleted 1972)]
Accepted name: hyaluronoglucosaminidase
Reaction: Random hydrolysis of (1→4)-linkages between N-acetyl-β-D-glucosamine and D-glucuronate residues in hyaluronate
For diagram click here.
Other name(s): hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I
Systematic name: hyaluronate 4-glycanohydrolase
Comments: Also hydrolyses (1→4)-β-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37326-33-3
References:
1. Meyer, K., Hoffman, P. and Linker, A. Hyaluronidases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 447-460.
2. Rapport, M.M., Myer, K. and Linker, A. Analysis of the products formed on hydrolysis of hyaluronic acid by testicular hyaluronidase. J. Am. Chem. Soc. 73 (1951) 2416-2420.
3. Weissmann, B. The transglycosylative action of testicular hyaluronidase. J. Biol. Chem. 216 (1955) 783-794.
Accepted name: hyaluronoglucuronidase
Reaction: Random hydrolysis of (1→3)-linkages between β-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate
Other name(s): hyaluronidase; glucuronoglucosaminoglycan hyaluronate lyase; orgelase
Systematic name: hyaluronate 3-glycanohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37288-34-9
References:
1. Linker, A., Meyer, K. and Hoffman, P. The production of hyaluronate oligosaccharides by leech hyaluronidase and alkali. J. Biol. Chem. 235 (1960) 924-927.
2. Meyer, K., Hoffman, P. and Linker, A. Hyaluronidases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 447-460.
Accepted name: xylan 1,4-β-xylosidase
Reaction: Hydrolysis of (1→4)-β-D-xylans, to remove successive D-xylose residues from the non-reducing termini
Other name(s): xylobiase; β-xylosidase; exo-1,4-β-xylosidase; β-D-xylopyranosidase; β-xylosidase; β-xylosidase; exo-1,4-xylosidase; exo-1,4-β-D-xylosidase; 1,4-β-D-xylan xylohydrolase
Systematic name: 4-β-D-xylan xylohydrolase
Comments: Also hydrolyses xylobiose. Some other exoglycosidase activities have been found associated with this enzyme in sheep liver.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-53-0
References:
1. Chinchetru, M.A., Cabezas, J.A. and Calvo, P. Purification and characterization of a broad specificity β-glucosidase from sheep liver. Int. J. Biochem. 21 (1989) 469-476. [PMID: 2503402]
2. Howard, B.H., Jones, G. and Purdom, M.R. The pentosanases of some rumen bacteria. Biochem. J. 74 (1960) 173-180.
Accepted name: β-D-fucosidase
Reaction: Hydrolysis of terminal non-reducing β-D-fucose residues in β-D-fucosides
Other name(s): β-fucosidase
Systematic name: β-D-fucoside fucohydrolase
Comment: Enzymes from some sources also hydrolyse β-D-galactosides and/or β-D-glucosides and/or α-L-arabinosides. The activity of EC 3.2.1.37 xylan 1,4-β-xylosidase, is an associated activity found in some sources (e.g. liver)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9025-34-7
References:
1. Chinchetru, M.A., Cabezas, J.A. and Calvo, P. Characterization and kinetics of β-D-gluco/fuco/galactosidase from sheep liver. Comp. Biochem. Physiol. B 75 (1983) 719-728. [PMID: 6413126]
2. Chinchetru, M.A., Cabezas, J.A. and Calvo, P. Purification and characterization of a broad specificity β-glucosidase from sheep liver. Int. J. Biochem. 21 (1989) 469-476. [PMID: 2503402]
3. Rodriguez, J.A., Cabezas, J.A. and Calvo, P. β-Fucosidase, β-glucosidase and β-galactosidase activities associated in bovine liver. Int. J. Biochem. 14 (1982) 695-698. [PMID: 6811346]
4. Wiederschain, G. and Prokopenkov, A. β-D-Galactosidase and β-D-fucosidase of pig kidney. Arch. Biochem. Biophys. 158 (1973) 539-543. [PMID: 4782520]
5. Wiederschain, G.Y., Beyer, E.M., Klyaschitsty, B.A. and Shashkov, A.S. Specificity patterns of different types of human fucosidase. Recognition of a certain region of the pyranose ring in sugars by the enzymes. Biochim. Biophys. Acta 659(1981) 434-444. [PMID: 6789883]
Accepted name: glucan endo-1,3-β-D-glucosidase
Reaction: Hydrolysis of (1→3)-β-D-glucosidic linkages in (1→3)-β-D-glucans
Other name(s): endo-1,3-β-glucanase; laminarinase; laminaranase; oligo-1,3-glucosidase; endo-1,3-β-glucanase; callase; β-1,3-glucanase; kitalase; 1,3-β-D-glucan 3-glucanohydrolase; endo-(1,3)-β-D-glucanase; (1→3)-β-glucan 3-glucanohydrolase; endo-1,3-β-D-glucanase; endo-1,3-β-glucosidase; 1,3-β-D-glucan glucanohydrolase
Systematic name: 3-β-D-glucan glucanohydrolase
Comments: Different from EC 3.2.1.6 endo-1,3(4)-β-glucanase. Very limited action on mixed-link (1,3-1,4-)-β-D-glucans. Hydrolyses laminarin, paramylon and pachyman.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-37-0
References:
1. Chesters, C.G.C. and Bull, A.T. The enzymic degradation of laminarin. 2. The multicomponent nature of fungal laminarinases. Biochem. J. 86 (1963) 31-38.
2. Reese, E.T. and Mandels, M. β-D-1,3-Glucanases in fungi. Can. J. Microbiol. 5 (1959) 173-185.
Accepted name: α-L-rhamnosidase
Reaction: Hydrolysis of terminal non-reducing α-L-rhamnose residues in α-L-rhamnosides
Other name(s): α-L-rhamnosidase T; α-L-rhamnosidase N
Systematic name: α-L-rhamnoside rhamnohydrolase
Comments: The enzyme, found in animal tissues, plants, yeasts, fungi and bacteria, utilizes an inverting mechanism of hydrolysis, releasing β-L-rhamnose. Substrates include naringin, rutin, quercitrin, hesperidin, dioscin, terpenyl glycosides and many other natural glycosides containing terminal α-L-rhamnose.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37288-35-0
References:
1. Rosenfeld, E. and Wiederschein, G. The metabolism of L-rhamnose in animal tissues. Bull. Soc. Chim. Biol. 47 (1965) 1433-1440. [PMID: 5855461]
2. Kurosawa, Y., Ikeda, K. and Egami, F. α-L-rhamnosidases of the liver of Turbo cornutus and Aspergillus niger. J. Biochem. 73 (1973) 31-37. [PMID: 4632197]
3. Zverlov, V.V., Hertel, C., Bronnenmeier, K., Hroch, A., Kellermann, J. and Schwarz, W.H. The thermostable α-L-rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial α-L-rhamnoside hydrolase, a new type of inverting glycoside hydrolase. Mol. Microbiol. 35 (2000) 173-179. [PMID: 10632887]
4. Yanai, T. and Sato, M. Purification and characterization of an α-L-rhamnosidase from Pichia angusta X349. Biosci. Biotechnol. Biochem. 64 (2000) 2179-2185. [PMID: 11129592]
5. Cui, Z., Maruyama, Y., Mikami, B., Hashimoto, W. and Murata, K. Crystal structure of glycoside hydrolase family 78 α-L-Rhamnosidase from Bacillus sp. GL1. J. Mol. Biol. 374 (2007) 384-398. [PMID: 17936784]
6. Rabausch, U., Ilmberger, N. and Streit, W.R. The metagenome-derived enzyme RhaB opens a new subclass of bacterial B type α-L-rhamnosidases. J. Biotechnol. 191 (2014) 38-45. [PMID: 24815685]
Accepted name: pullulanase
Reaction: Hydrolysis of (1→6)-α-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the α- and β-limit dextrins of amylopectin and glycogen
Glossary: pullulan = a linear polymer of 1→6-linked maltotriose units.
Other name(s): limit dextrinase (erroneous); amylopectin 6-glucanohydrolase; bacterial debranching enzyme; debranching enzyme; α-dextrin endo-1,6-α-glucosidase; R-enzyme; pullulan α-1,6-glucanohydrolase
Systematic name: pullulan 6-α-glucanohydrolase
Comments: Different from EC 3.2.1.142 (limit dextrinase) in its action on glycogen, and its rate of hydrolysis of limit dextrins. Its action on amylopectin is complete. Maltose is the smallest sugar that it can release from an α-(1<→6)-linkage.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9075-68-7
References:
1. Lee, E.Y.C. and Whelan, W.J. Glycogen and starch debranching enzymes, in Boyer, P.D. (Ed.), The Enzymes, 3rd edn., vol. 5, Academic Press, New York, 1972, pp. 191-234.
2. Bender, H. and Wallenfels, K. Pullulanase (an amylopectin and glycogen debranching enzyme) from Aerobacter aerogenes. Methods Enzymol. 8 (1966) 555-559.
3. Manners, D.J. Observations on the specificity and nomenclature of starch debranching enzymes. J. Appl. Glycosci. 44 (1997) 83-85.
Accepted name: GDP-glucosidase
Reaction: GDP-glucose + H2O = D-glucose + GDP
Other name(s): guanosine diphosphoglucosidase; guanosine diphosphate D-glucose glucohydrolase
Systematic name: GDP-glucose glucohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37288-36-1
References:
1. Sonnino, S., Carinatti, H. and Cabib, E. Guanosine diphosphate D-glucose glucohydrolase. Arch. Biochem. Biophys. 116 (1966) 26-33. [PMID: 5963308]
Accepted name: β-L-rhamnosidase
Reaction: Hydrolysis of terminal, non-reducing β-L-rhamnose residues in β-L-rhamnosides
Systematic name: β-L-rhamnoside rhamnohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37288-37-2
References:
1. Barker, S.A., Somers, P.J. and Stacey, M. Arrangement of the L-rhamnose units in Diplococcus pneumoniae type II polysaccharide. Carbohydr. Res. 1 (1965) 106-115.
[EC 3.2.1.44 Transferred entry: fucoidanase. Now EC 3.2.1.211, endo-(13)-fucoidanase and EC 3.2.1.212, endo-(14)-fucoidanase (EC 3.2.1.44 created 1972, deleted 2020)]
Accepted name: glucosylceramidase
Reaction: a D-glucosyl-N-acylsphingosine + H2O = D-glucose + an N-acylsphingosine
For diagram of the reaction click here.
Other name(s): psychosine hydrolase; glucosphingosine glucosylhydrolase; GlcCer-β-glucosidase; β-D-glucocerebrosidase; glucosylcerebrosidase; β-glucosylceramidase; ceramide glucosidase; glucocerebrosidase; glucosylsphingosine β-glucosidase; glucosylsphingosine β-D-glucosidase
Systematic name: D-glucosyl-N-acylsphingosine glucohydrolase
Comments: Also acts on glucosylsphingosine (cf. EC 3.2.1.62 glycosylceramidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37228-64-1
References:
1. Brady, R.O., Kanfer, J.N. and Shapiro, D. The metabolism of glucocerebrosides. I. Preparation and properties of a glucocerebroside-cleaving enzyme from spleen tissue. J. Biol. Chem. 240 (1966) 39-43.
2. Vaccaro, A.M., Muscillo, M. and Suzuki, K. Characterization of human glucosylsphingosine glucosyl hydrolase and comparison with glucosylceramidase. Eur. J. Biochem. 146 (1985) 315-321. [PMID: 3967661]
Accepted name: galactosylceramidase
Reaction: a D-galactosyl-N-acylsphingosine + H2O = D-galactose + an N-acylsphingosine
Other name(s): cerebroside galactosidase; galactocerebroside.β-galactosidase; galactosylcerebrosidase; galactocerebrosidase; ceramide galactosidase; galactocerebroside galactosidase; galactosylceramide.β-galactosidase; cerebroside β-galactosidase; galactosylceramidase I; β-galactosylceramidase; galactocerebroside-β-D-galactosidase; lactosylceramidase I; β-galactocerebrosidase; lactosylceramidase
Systematic name: D-galactosyl-N-acylsphingosine galactohydrolase
Comments: cf. EC 3.2.1.62 glycosylceramidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-89-8
References:
1. Brady, R.O., Gal, A.E., Kanfer, J.N. and Bradley, R.M. The metabolism of glucocerebrosides. 3. Purification and properties of a glucosyl- and galactosylceramide-cleaving enzyme from rat intestinal tissue. J. Biol. Chem. 240 (1965) 3766-3770. [PMID: 5320641]
Deleted entry: galactosylgalactosylglucosylceramidase. Now known to be catalyzed by EC 3.2.1.22, α-galactosidase.
Accepted name: sucrose α-glucosidase
Reaction: Hydrolysis of sucrose and maltose by an α-D-glucosidase-type action
Other name(s): sucrose α-glucohydrolase; sucrase; sucrase-isomaltase; sucrose.alpha.-glucohydrolase; intestinal sucrase; sucrase(invertase)
Systematic name: sucrose-α-D-glucohydrolase
Comments: This enzyme is isolated from intestinal mucosa as a single polypeptide chain that also displays activity towards isomaltose (EC 3.2.1.10 oligo-1,6-glucosidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37288-39-4
References:
1. Conklin, K.A., Yamashiro, K.M. and Gray, G.M. Human intestinal sucrase-isomaltase. Identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits. J. Biol. Chem. 250 (1975) 5735-5741. [PMID: 807575]
2. Hauri, H.-P., Quaroni, A. and Isselbacher, K.J. Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase. Proc. Natl. Acad. Sci. USA 76 (1979) 5183-5186. [PMID: 291933]
3. Kolinska, J. and Kraml, J. Separation and characterization of sucrose-isomaltase and of glucoamylase of rat intestine. Biochim. Biophys. Acta 284 (1972) 235-247. [PMID: 5073761]
4. Sigrist, H., Ronner, P. and Semenza, G. A hydrophobic form of the small-intestinal sucrase-isomaltase complex. Biochim. Biophys. Acta 406 (1975) 433-446. [PMID: 1182172]
5. Sjöström, H., Norén, O., Christiansen, L., Wacker, H. and Semenza, G. A fully active, two-active-site, single-chain sucrase.isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein. J. Biol. Chem. 255 (1980) 11332-11338. [PMID: 7002920]
6. Takesue, Y. Purification and properties of rabbit intestinal sucrase. J. Biochem. (Tokyo) 65 (1969) 545-552. [PMID: 5804876]
Accepted name: α-N-acetylgalactosaminidase
Reaction: Cleavage of non-reducing α-(1→3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids
Other name(s): α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase
Systematic name: α-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase
Comments: The human lysosomal enzyme is involved in the degradation of blood type A epitope.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9075-63-2
References:
1. Asfaw, B., Schindler, D., Ledvinova, J., Cerny, B., Smid, F. and Conzelmann, E. Degradation of blood group A glycolipid A-6-2 by normal and mutant human skin fibroblasts. J. Lipid Res. 39 (1998) 1768-1780. [PMID: 9741689]
2. Zhu, A., Monahan, C., Wang, Z.K. and Goldstein, J. Expression, purification, and characterization of recombinant α-N-acetylgalactosaminidase produced in the yeast Pichia pastoris. Protein Expr. Purif. 8 (1996) 456-462. [PMID: 8954893]
3. Clark, N.E. and Garman, S.C. The 1.9 Å structure of human α-N-acetylgalactosaminidase: The molecular basis of Schindler and Kanzaki diseases. J. Mol. Biol. 393 (2009) 435-447. [PMID: 19683538]
4. Hoskins, L.C., Boulding, E.T. and Larson, G. Purification and characterization of blood group A-degrading isoforms of α-N-acetylgalactosaminidase from Ruminococcus torques strain IX-70. J. Biol. Chem. 272 (1997) 7932-7939. [PMID: 9065462]
5. Harun-Or-Rashid, M., Matsuzawa, T., Satoh, Y., Shiraishi, T., Ando, M., Sadik, G. and Uda, Y. Purification and characterization of α-N-acetylgalactosaminidases I and II from the starfish Asterina amurensis. Biosci. Biotechnol. Biochem. 74 (2010) 256-261. [PMID: 20139603]
6. Weignerova, L., Filipi, T., Manglova, D. and Kren, V. Induction, purification and characterization of α-N-acetylgalactosaminidase from Aspergillus niger. Appl. Microbiol. Biotechnol. 79 (2008) 769-774. [PMID: 18443780]
7. Ashida, H., Tamaki, H., Fujimoto, T., Yamamoto, K. and Kumagai, H. Molecular cloning of cDNA encoding α-N-acetylgalactosaminidase from Acremonium sp. and its expression in yeast. Arch. Biochem. Biophys. 384 (2000) 305-310. [PMID: 11368317]
Accepted name: α-N-acetylglucosaminidase
Reaction: Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-α-D-glucosaminides
Other name(s): α-acetylglucosaminidase; N-acetyl-α-D-glucosaminidase; N-acetyl-α-glucosaminidase; α-D-2-acetamido-2-deoxyglucosidase
Systematic name: α-N-acetyl-D-glucosaminide N-acetylglucosaminohydrolase
Comments: Hydrolyses UDP-N-acetylglucosamine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37288-40-7
References:
1. von Figura, K. Human α-N-acetylglucosaminidase. 1. Purification and properties. Eur. J. Biochem. 80 (1977) 523-533. [PMID: 411658]
2. von Figura, K. Human α-N-acetylglucosaminidase. 2. Activity towards natural substrates and multiple recognition forms. Eur. J. Biochem. 80 (1977) 535-542. [PMID: 923593]
3. Weissmann, B., Rowen, G., Marshall, J. and Friederici, D. Mammalian α-acetylglucosaminidase. Enzymic properties, tissue distribution, and intracellular localization. Biochemistry 6 (1967) 207-214. [PMID: 4291567]
4. Werries, E., Wollek, E., Gottschalk, A. and Buddecke, E. Separation of N-acetyl-α-glucosaminidase and N-acetyl-α-galactosaminidase from ox spleen. Cleavage of the O-glycosidic linkage between carbohydrate and polypeptide in ovine and bovine submaxillary glycoprotein by N-acetyl-α-galactosaminidase. Eur. J. Biochem. 10 (1969) 445-449. [PMID: 5348072]