EC |
3.2.1.149 | Relevance: 100% |
Accepted name: |
β-primeverosidase |
Reaction: |
a 6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside + H2O = 6-O-(β-D-xylopyranosyl)-β-D-glucopyranose + an alcohol |
Glossary: |
primeverose = 6-O-(β-D-xylopyranosyl)-D-glucose
vicianose = 6-O-(α-L-arabinopyranosyl)-D-glucose |
Systematic name: |
6-O-(β-D-xylopyranosyl)-β-D-glucopyranoside 6-O-(β-D-xylosyl)-β-D-glucohydrolase |
Comments: |
The enzyme is responsible for the formation of the alcoholic aroma in oolong and black tea. In addition to β-primeverosides [i.e. 6-O-(β-D-xylopyranosyl)-β-D-glucopyranosides], it also hydrolyses 6-O-(β-D-apiofuranosyl)-β-D-glucopyranosides and, less rapidly, β-vicianosides and 6-O-(α-L-arabinofuranosyl)-β-D-glucopyranosides, but not β-glucosides. Geranyl-, linaloyl-, benzyl- and p-nitrophenol glycosides are all hydrolysed. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 884593-92-4 |
References: |
1. |
Ijima, Y., Ogawa, K., Watanabe, N., Usui, T., Ohnishi-Kameyama, M., Nagata, T. and Sakata, K. Characterization of β-primeverosidase, being concerned with alcoholic aroma formation in tea leaves to be processed into black tea, and preliminary observations on its substrate specificity. J. Agric. Food Chem. 46 (1998) 1712–1718. |
2. |
Ogawa, K., Ijima, Y., Guo, W., Watanabe, N., Usui, T., Dong, S., Tong, Q. and Sakata, K. Purification of a β-primeverosidase concerned with alcoholic aroma formation in tea leaves (cv. Shuxian) to be processed to oolong tea. J. Agric. Food Chem. 45 (1997) 877–882. |
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[EC 3.2.1.149 created 2001] |
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EC |
3.2.1.21 | Relevance: 96.9% |
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. [PMID: 13230003] |
3. |
Dahlqvist, A. Pig intestinal β-glucosidase activities. I. Relation to β-galactosidase (lactase). Biochim. Biophys. Acta 50 (1961) 55–61. [DOI] [PMID: 13719334] |
4. |
Heyworth, R. and Walker, P.G. Almond-emulsin β-D-glucosidase and β-D-galactosidase. Biochem. J. 83 (1962) 331–335. [PMID: 13907157] |
5. |
Larner, J. Other glucosidases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), 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. [DOI] [PMID: 235305] |
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[EC 3.2.1.21 created 1961] |
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|
EC |
3.2.1.140 | Relevance: 96.3% |
Accepted name: |
lacto-N-biosidase |
Reaction: |
β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-D-Glc + H2O = β-D-Gal-(1→3)-D-GlcNAc + β-D-Gal-(1→4)-D-Glc |
Glossary: |
β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-D-Glc = lacto-N-tetraose
β-D-Gal-(1→3)-D-GlcNAc = lacto-N-biose
β-D-Gal-(1→4)-D-Glc = lactose |
Systematic name: |
oligosaccharide lacto-N-biosylhydrolase |
Comments: |
The enzyme from Streptomyces specifically hydrolyses the terminal lacto-N-biosyl residue (β-D-Gal-(1→3)-D-GlcNAc) from the non-reducing end of oligosaccharides with the structure β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→R). Lacto-N-hexaose (β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-D-Glc) is hydrolysed to form first lacto-N-tetraose plus lacto-N-biose, with the subsequent formation of lactose. Oligosaccharides in which the non-reducing terminal Gal or the penultimate GlcNAc are replaced by fucose or sialic acid are not substrates. Asialo GM1 tetraose (β-D-Gal-(1→3)-β-D-GalNAc-(1→3)-β-D-Gal-(1→4)-D-Glc) is hydrolysed very slowly, but lacto-N-neotetraose (β-D-Gal-(1→4)-β-D-GalNAc-(1→3)-β-D-Gal-(1→4)-D-Glc) is not a substrate |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 146359-52-6 |
References: |
1. |
Sano, M., Hayakawa, K., Kato, I. An enzyme releasing lacto-N-biose from oligosaccharides. Proc. Natl. Acad. Sci. USA 89 (1992) 8512–8516. [DOI] [PMID: 1528855] |
2. |
Sano, M., Hayakawa, K., Kato, I. Purification and characterization of an enzyme releasing lacto-N-biose from oligosaccharides with type 1 chain. J. Biol. Chem. 268 (1993) 18560–18566. [PMID: 7689556] |
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[EC 3.2.1.140 created 1999] |
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EC
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2.4.1.163
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Transferred entry: | β-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,3-acetylglucosaminyltransferase, now included in EC 2.4.1.149, N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase
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[EC 2.4.1.163 created 1989, deleted 2016] |
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EC |
2.5.1.98 | Relevance: 95.5% |
Accepted name: |
Rhizobium leguminosarum exopolysaccharide glucosyl ketal-pyruvate-transferase |
Reaction: |
phosphoenolpyruvate + [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n = [β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-(CH3CH(OH)CH2C(O))-4,6-CH3(COO-)C-β-D-Gal-(1→3)-4,6-CH3(COO-)C-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n + phosphate
|
Other name(s): |
PssM; phosphoenolpyruvate:[D-GlcA-β-(1→4)-2-O-Ac-D-GlcA-β-(1→4)-D-Glc-β-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-D-Gal-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→4)-D-Glc-β-(1→6)]-2(or 3)-O-Ac-D-Glc-α-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase |
Systematic name: |
phosphoenolpyruvate:[β-D-GlcA-(1→4)-2-O-Ac-β-D-GlcA-(1→4)-β-D-Glc-(1→4)-[3-O-CH3-CH2CH(OH)C(O)-4,6-CH3(COO-)C-β-D-Gal-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→4)-β-D-Glc-(1→6)]-2(or 3)-O-Ac-α-D-Glc-(1→6)]n 4,6-O-(1-carboxyethan-1,1-diyl)transferase |
Comments: |
The enzyme is responsible for pyruvylation of the subterminal glucose in the acidic octasaccharide repeating unit of the exopolysaccharide of Rhizobium leguminosarum (bv. viciae strain VF39) which is necessary to establish nitrogen-fixing symbiosis with Pisum sativum, Vicia faba, and Vicia sativa. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ivashina, T.V., Fedorova, E.E., Ashina, N.P., Kalinchuk, N.A., Druzhinina, T.N., Shashkov, A.S., Shibaev, V.N. and Ksenzenko, V.N. Mutation in the pssM gene encoding ketal pyruvate transferase leads to disruption of Rhizobium leguminosarum bv. viciae—Pisum sativum symbiosis. J. Appl. Microbiol. 109 (2010) 731–742. [DOI] [PMID: 20233262] |
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[EC 2.5.1.98 created 2012, modified 2018] |
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EC |
3.2.1.6 | Relevance: 94.6% |
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(or 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. [DOI] [PMID: 5354264] |
2. |
Barras, D.R. and Stone, B.A. β-1,3-Glucan hydrolases from Euglena gracilis. II. Purification and properties of the β-1,3-glucan exo-hydrolase. Biochim. Biophys. Acta 191 (1969) 342–353. [DOI] [PMID: 5354265] |
3. |
Cunningham, L.W. and Manners, D.J. Enzymic degradation of lichenin. Biochem. J. 80 (1961) 42. |
4. |
Reese, E.T. and Mandels, M. β-D-1,3-Glucanases in fungi. Can. J. Microbiol. 5 (1959) 173–185. [PMID: 13638895] |
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. [DOI] [PMID: 5500926] |
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[EC 3.2.1.6 created 1961, modified 1976] |
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EC |
3.2.1.187 | Relevance: 93.5% |
Accepted name: |
(Ara-f)3-Hyp β-L-arabinobiosidase |
Reaction: |
4-O-(β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + H2O = 4-O-(β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranose |
Glossary: |
4-O-(β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline = (Ara-f)3-Hyp |
Other name(s): |
hypBA2 (gene name); β-L-arabinobiosidase |
Systematic name: |
4-O-(β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranose hydrolase |
Comments: |
The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, is specific for (Ara-f)3-Hyp, a sugar chain found in hydroxyproline-rich glyoproteins such as extensin and lectin. The enzyme was not able to accept (Ara-f)2-Hyp or (Ara-f)4-Hyp as substrates. In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Fujita, K., Sakamoto, S., Ono, Y., Wakao, M., Suda, Y., Kitahara, K. and Suganuma, T. Molecular cloning and characterization of a β-L-Arabinobiosidase in Bifidobacterium longum that belongs to a novel glycoside hydrolase family. J. Biol. Chem. 286 (2011) 5143–5150. [DOI] [PMID: 21149454] |
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[EC 3.2.1.187 created 2013] |
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EC |
2.4.1.386 | Relevance: 93.4% |
Accepted name: |
GlcNAc-β-1,3-Gal β-1,6-N-acetylglucosaminyltransferase (distally acting) |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-R = UDP + β-D-GlcNAc-(1→3)-[β-D-GlcNAc-(1→6)]-β-D-Gal-(1→4)-β-D-GlcNAc-R |
Other name(s): |
UDP-GlcNAc:GlcNAcβ1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase; dIGnT; C2GnT2 (misleading) |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminide 6-β-N-acetylglucosaminyltransferase (configuration-inverting) |
Comments: |
Involved in the production of milk oligosaccharides in the lacto-N-triose (LNT) series. Cf. EC 2.4.1.150 (N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase; cIGnT) and EC 2.4.1.148 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85638-40-0 |
References: |
1. |
Piller, F., Cartron, J.P., Maranduba, A., Veyrieres, A., Leroy, Y. and Fournet, B. Biosynthesis of blood group I antigens. Identification of a UDP-GlcNAc:GlcNAc β1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase in hog gastric mucosa. J. Biol. Chem. 259 (1984) 13385–13390. [PMID: 6490658] |
2. |
Yeh, J.C., Ong, E. and Fukuda, M. Molecular cloning and expression of a novel β-1,6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J. Biol. Chem. 274 (1999) 3215–3221. [DOI] [PMID: 9915862] |
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[EC 2.4.1.386 created 2021] |
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EC |
3.2.1.52 | Relevance: 93.2% |
Accepted name: |
β-N-acetylhexosaminidase |
Reaction: |
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-β-D-hexosaminides |
Other name(s): |
hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-β-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhexosaminidase; β-N-acetyl-D-hexosaminidase; β-N-acetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase; β-D-hexosaminidase; NAHase |
Systematic name: |
β-N-acetyl-D-hexosaminide N-acetylhexosaminohydrolase |
Comments: |
Acts on N-acetylglucosides and N-acetylgalactosides. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-33-3 |
References: |
1. |
Cabezas, J.A. Some comments on the type references of the official nomenclature (IUB) for β-N-acetylglucosaminidase, β-N-acetylhexosaminidase and β-N-acetylgalactosaminidase. Biochem. J. 261 (1989) 1059–1060. [PMID: 2529847] |
2. |
Calvo, P., Reglero, A. and Cabezas, J.A. Purification and properties of β-N-acetylhexosaminidase from the mollusc Helicella ericetorum Muller. Biochem. J. 175 (1978) 743–750. [PMID: 33660] |
3. |
Frohwein, Y.S. and Gatt, S. Isolation of β-N-acetylhexosaminidase, β-N-acetylglucosaminidase, and β-N-acetylgalactosaminidase from calf brain. Biochemistry 6 (1967) 2775–2782. [PMID: 6055190] |
4. |
Li, S.-C. and Li, Y.-T. Studies on the glycosidases of jack bean meal. 3. Crystallization and properties of β-N-acetylhexosaminidase. J. Biol. Chem. 245 (1970) 5153–5160. [PMID: 5506280] |
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[EC 3.2.1.52 created 1972 (EC 3.2.1.30 created 1961, incorporated 1992 [EC 3.2.1.29 created 1961, incorporated 1972])] |
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EC |
2.4.1.226 | Relevance: 93% |
Accepted name: |
N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase |
Reaction: |
(1) UDP-α-D-glucuronate + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine (2) UDP-α-D-glucuronate + [protein]-3-O-([β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-[β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine |
|
For diagram of chondroitin biosynthesis (later stages), click here |
Other name(s): |
chondroitin glucuronyltransferase II; α-D-glucuronate:N-acetyl-β-D-galactosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 3-β-glucuronosyltransferase; UDP-α-D-glucuronate:N-acetyl-β-D-galactosaminyl-(1→4)-β-D-glucuronosyl-proteoglycan 3-β-glucuronosyltransferase |
Systematic name: |
UDP-α-D-glucuronate:[protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 3-β-glucuronosyltransferase (configuration-inverting) |
Comments: |
Involved in the biosynthesis of chondroitin and dermatan sulfate. The human chondroitin synthetase is a bifunctional glycosyltransferase, which has the 3-β-glucuronosyltransferase and 4-β-N-acetylgalactosaminyltransferase (EC 2.4.1.175) activities required for the synthesis of the chondroitin sulfate disaccharide repeats. Similar chondroitin synthase ’co-polymerases’ can be found in Pasteurella multocida and Escherichia coli. There is also another human protein with apparently only the 3-β-glucuronosyltransferase activity. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 269077-98-7 |
References: |
1. |
Kitagawa, H., Uyama, T. and Sugahara, K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721–38726. [DOI] [PMID: 11514575] |
2. |
DeAngelis, P.L. and Padgett-McCue, A.J. Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F. J. Biol. Chem. 275 (2000) 24124–24129. [DOI] [PMID: 10818104] |
3. |
Ninomiya, T., Sugiura, N., Tawada, A., Sugimoto, K., Watanabe, H. and Kimata, K. Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4. J. Biol. Chem. 277 (2002) 21567–21575. [DOI] [PMID: 11943778] |
4. |
Gotoh, M., Yada, T., Sato, T., Akashima, T., Iwasaki, H., Mochizuki, H., Inaba, N., Togayachi, A., Kudo, T., Watanabe, H., Kimata, K. and Narimatsu, H. Molecular cloning and characterization of a novel chondroitin sulfate glucuronyltransferase which transfers glucuronic acid to N-acetylgalactosamine. J. Biol. Chem. 277 (2002) 38179–38188. [DOI] [PMID: 12145278] |
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[EC 2.4.1.226 created 2002, modified 2018] |
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EC |
3.5.2.6 | Relevance: 92.9% |
Accepted name: |
β-lactamase |
Reaction: |
a β-lactam + H2O = a substituted β-amino acid |
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For diagram of penicillin biosynthesis and metabolism, click here |
Other name(s): |
penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I; penicillinase II; β-lactamase I; β-lactamase II; β-lactamase III; β-lactamase A; β-lactamase B; β-lactamase C; β-lactamase AME I; cephalosporin-β-lactamase; carbapenemase |
Systematic name: |
β-lactam hydrolase |
Comments: |
A group of enzymes of varying specificity hydrolysing β-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9073-60-3 |
References: |
1. |
Citri, N. Penicillinase and other β-lactamases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 4, Academic Press, New York, 1971, pp. 23–46. |
2. |
Hennessey, T.D. and Richmond, M.H. The purification and some properties of a β-lactamase (cephalosporinase) synthesized by Enterobacter cloacae. Biochem. J. 109 (1968) 469–473. [PMID: 5685878] |
3. |
Kuwabara, S. Purification and properties of two extracellular β-lactamases from Bacillus cereus 569-H. Biochem. J. 118 (1970) 457–465. [PMID: 4990588] |
4. |
Pollock, M.R. Penicillinase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 269–278. |
5. |
Pollock, M.R., Torriani, A.-M. and Tridgell, E.G. Crystalline bacterial penicillinase. Biochem. J. 62 (1956) 387–391. [PMID: 13303985] |
6. |
Ross, G.W. and Boulton, M.G. Purification of β-lactamases on QAE-sephadex. Biochim. Biophys. Acta 309 (1973) 430–439. [DOI] [PMID: 4731970] |
|
[EC 3.5.2.6 created 1961, modified 1981 (EC 3.5.2.8 created 1972, incorporated 1978)] |
|
|
|
|
EC |
3.2.1.74 | Relevance: 92.8% |
Accepted name: |
glucan 1,4-β-glucosidase |
Reaction: |
Hydrolysis of (1→4)-linkages in (1→4)-β-D-glucans, to remove successive glucose units |
Other name(s): |
exo-1,4-β-glucosidase; exocellulase; exo-β-1,4-glucosidase; exo-β-1,4-glucanase; β-1,4-β-glucanase; β-glucosidase; exo-1,4-β-glucanase; 1,4-β-D-glucan glucohydrolase |
Systematic name: |
4-β-D-glucan glucohydrolase |
Comments: |
Acts on 1,4-β-D-glucans and related oligosaccharides. Cellobiose is hydrolysed, but very slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-52-1 |
References: |
1. |
Barras, D.R., Moore, A.E. and Stone, B.A. Enzyme-substrate relations among β-glucan hydrolases. Adv. Chem. Ser. 95 (1969) 105–138. |
|
[EC 3.2.1.74 created 1972] |
|
|
|
|
EC |
3.2.1.37 | Relevance: 91.9% |
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. [PMID: 14403433] |
|
[EC 3.2.1.37 created 1965] |
|
|
|
|
EC |
3.2.1.75 | Relevance: 91.8% |
Accepted name: |
glucan endo-1,6-β-glucosidase |
Reaction: |
Random hydrolysis of (1→6)-linkages in (1→6)-β-D-glucans |
Other name(s): |
endo-1,6-β-glucanase; β-1→6)-β-D-glucanase; β-1,6-glucanase-pustulanase; β-1,6-glucan hydrolase; β-1,6-glucan 6-glucanohydrolase; 1,6-β-D-glucan glucanohydrolase |
Systematic name: |
6-β-D-glucan glucanohydrolase |
Comments: |
Acts on lutean, pustulan and 1,6-oligo-β-D-glucosides. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-39-0 |
References: |
1. |
Reese, E.T., Parrish, F.W. and Mandels, M. β-D-1,6-Glucanases in fungi. Can. J. Microbiol. 8 (1962) 327–334. [PMID: 14491003] |
|
[EC 3.2.1.75 created 1972] |
|
|
|
|
EC
|
2.4.1.164
|
Transferred entry: | galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide β-1,6-N-acetylglucosaminyltransferase, now included with EC 2.4.1.150, N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase
|
[EC 2.4.1.164 created 1989, deleted 2016] |
|
|
|
|
EC |
3.2.1.38 | Relevance: 91.1% |
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 |
Comments: |
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. [DOI] [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. [DOI] [PMID: 6789883] |
|
[EC 3.2.1.38 created 1965, deleted 1972, reinstated 1978] |
|
|
|
|
EC |
3.2.1.23 | Relevance: 89.8% |
Accepted name: |
β-galactosidase |
Reaction: |
Hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides |
Other name(s): |
lactase (ambiguous); 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. [PMID: 13426167] |
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. [PMID: 14943665] |
7. |
Wallenfels, K. and Malhotra, O.P. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), 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] |
|
[EC 3.2.1.23 created 1961, modified 1980] |
|
|
|
|
EC |
2.4.1.135 | Relevance: 89.8% |
Accepted name: |
galactosylgalactosylxylosylprotein 3-β-glucuronosyltransferase |
Reaction: |
UDP-α-D-glucuronate + [protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine = UDP + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine |
|
For diagram of heparan and chondroitin biosynthesis (early stages), click here |
Glossary: |
[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = [protein]-3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine |
Other name(s): |
glucuronosyltransferase I; uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase; UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosyl-protein D-glucuronosyltransferase; UDP-glucuronate:3-β-D-galactosyl-4-β-D-galactosyl-O-β-D-xylosylprotein D-glucuronosyltransferase |
Systematic name: |
UDP-α-D-glucuronate:[protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine D-glucuronosyltransferase (configuration-inverting) |
Comments: |
Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 227184-75-0 |
References: |
1. |
Helting, J. and Roden, L. Biosynthesis of chondroitin sulfate. II. Glucuronosyl transfer in the formation of the carbohydrate-protein linkage region. J. Biol. Chem. 244 (1969) 2799–2805. [PMID: 5770003] |
2. |
Helting, T. Biosynthesis of heparin. Solubilization and partial purification of uridine diphosphate glucuronic acid: acceptor glucuronosyltransferase from mouse mastocytoma. J. Biol. Chem. 247 (1972) 4327–4332. [PMID: 4260846] |
3. |
Kitagawa, H., Tone, Y., Tamura, J., Neumann, K.W., Ogawa, T., Oka, S., Kawasaki, T. and Sugahara, K. Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J. Biol. Chem. 273 (1998) 6615–6618. [DOI] [PMID: 9506957] |
|
[EC 2.4.1.135 created 1984, modified 2002, modified 2016] |
|
|
|
|
EC |
2.4.1.174 | Relevance: 89.4% |
Accepted name: |
glucuronylgalactosylproteoglycan 4-β-N-acetylgalactosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-galactosamine + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine |
|
For diagram of chondroitin biosynthesis (later stages), click here |
Glossary: |
[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = [protein]-3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine |
Other name(s): |
N-acetylgalactosaminyltransferase I; glucuronylgalactosylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I; UDP-N-acetyl-D-galactosamine:D-glucuronyl-1,3-β-D-galactosyl-proteoglycan β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:D-glucuronyl-(1→3)-β-D-galactosyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase |
Systematic name: |
UDP-N-acetyl-D-galactosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4-β-N-acetylgalactosaminyltransferase (configuration-inverting) |
Comments: |
Requires Mn2+. Involved in the biosynthesis of chondroitin sulfate. Key enzyme activity for the initiation of chondroitin and dermatan sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 96189-39-8 |
References: |
1. |
Rohrmann, K., Niemann, R. and Buddecke, E. Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate. Eur. J. Biochem. 148 (1985) 463–469. [DOI] [PMID: 3922754] |
2. |
Uyama, T., Kitagawa, H., Tamura, J.-i. and Sugahara, K. Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: the key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate. J. Biol. Chem. 277 (2002) 8841–8846. [DOI] [PMID: 11788602] |
|
[EC 2.4.1.174 created 1989, modified 2002] |
|
|
|
|
EC |
3.2.1.39 | Relevance: 89% |
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. [PMID: 14020682] |
2. |
Reese, E.T. and Mandels, M. β-D-1,3-Glucanases in fungi. Can. J. Microbiol. 5 (1959) 173–185. [PMID: 13638895] |
|
[EC 3.2.1.39 created 1965] |
|
|
|
|
EC |
3.2.1.213 | Relevance: 88.9% |
Accepted name: |
galactan exo-1,6-β-galactobiohydrolase (non-reducing end) |
Reaction: |
Hydrolysis of (1→6)-β-D-galactosidic linkages in arabinogalactan proteins and (1→3):(1→6)-β-galactans to yield (1→6)-β-galactobiose as the final product. |
Other name(s): |
exo-β-1,6-galactobiohydrolase; 1,6Gal (gene name) |
Systematic name: |
exo-β-(1→6)-galactobiohydrolase (non-reducing end) |
Comments: |
The enzyme, characterized from the bacterium Bifidobacterium longum, specifically hydrolyses (1→6)-β-galactobiose from the non-reducing terminal of (1→6)-β-D-galactooligosaccharides with a degree of polymerization (DP) of 3 or higher, using an exo mode of action. The enzyme cannot hydrolyse α-L-arabinofuranosylated (1→6)-β-galactans (as found in arabinogalactans) and does not act on (1→3)-β-D- or (1→4)-β-D-galactans. cf. EC 3.2.1.164, galactan endo-1,6-β-galactosidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Fujita, K., Sakamoto, A., Kaneko, S., Kotake, T., Tsumuraya, Y. and Kitahara, K. Degradative enzymes for type II arabinogalactan side chains in Bifidobacterium longum subsp. longum. Appl. Microbiol. Biotechnol. 103 (2019) 1299–1310. [PMID: 30564851] |
|
[EC 3.2.1.213 created 2020] |
|
|
|
|
EC |
3.4.11.25 | Relevance: 88.8% |
Accepted name: |
β-peptidyl aminopeptidase |
Reaction: |
Cleaves N-terminal β-homoamino acids from peptides composed of 2 to 6 amino acids |
Other name(s): |
BapA (ambiguous) |
Comments: |
Sphingosinicella xenopeptidilytica strain 3-2W4 is able to utilize the β-peptides β-homoVal-β-homoAla-β-homoLeu and β-homoAla-β-homoLeu as sole carbon and energy sources [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB |
References: |
1. |
Heck, T., Limbach, M., Geueke, B., Zacharias, M., Gardiner, J., Kohler, H.P. and Seebach, D. Enzymatic degradation of β- and mixed α,β-oligopeptides. Chem. Biodivers. 3 (2006) 1325–1348. [DOI] [PMID: 17193247] |
2. |
Geueke, B., Namoto, K., Seebach, D. and Kohler, H.P. A novel β-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves
peptide bonds of synthetic β-tri- and β-dipeptides. J. Bacteriol. 187 (2005) 5910–5917. [DOI] [PMID: 16109932] |
3. |
Geueke, B., Heck, T., Limbach, M., Nesatyy, V., Seebach, D. and Kohler, H.P. Bacterial β-peptidyl aminopeptidases with unique substrate specificities for β-oligopeptides and mixed β,α-oligopeptides. FEBS J. 273 (2006) 5261–5272. [DOI] [PMID: 17064315] |
4. |
Heck, T., Kohler, H.P., Limbach, M., Flögel, O., Seebach, D. and Geueke, B. Enzyme-catalyzed formation of β-peptides: β-peptidyl aminopeptidases BapA and DmpA acting as β-peptide-synthesizing enzymes. Chem. Biodivers. 4 (2007) 2016. [DOI] [PMID: 17886858] |
|
[EC 3.4.11.25 created 2011] |
|
|
|
|
EC |
3.2.1.161 | Relevance: 88.6% |
Accepted name: |
β-apiosyl-β-glucosidase |
Reaction: |
7-[β-D-apiofuranosyl-(1→6)-β-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + β-D-apiofuranosyl-(1→6)-D-glucose |
Other name(s): |
isoflavonoid-7-O-β[D-apiosyl-(1→6)-β-D-glucoside] disaccharidase; isoflavonoid 7-O-β-apiosyl-glucoside β-glucosidase; furcatin hydrolase |
Systematic name: |
7-[β-D-apiofuranosyl-(1→6)-β-D-glucopyranosyloxy]isoflavonoid β-D-apiofuranosyl-(1→6)-D-glucohydrolase |
Comments: |
The enzyme from the tropical tree Dalbergia nigrescens Kurz belongs in glycosyl hydrolase family 1. The enzyme removes disaccharides from the natural substrates dalpatein 7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside and 7-hydroxy-2′,4′,5′,6-tetramethoxy-7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside (dalnigrein 7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside) although it can also remove a single glucose residue from isoflavonoid 7-O-glucosides [2]. Daidzin and genistin are also substrates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 1000598-83-3 |
References: |
1. |
Hosel, W. and Barz, W. β-Glucosidases from Cicer arietinum L. Purification and Properties of
isoflavone-7-O-glucoside-specific β-glucosidases. Eur. J. Biochem. 57 (1975) 607–616. [DOI] [PMID: 240725] |
2. |
Chuankhayan, P., Hua, Y., Svasti, J., Sakdarat, S., Sullivan, P.A. and Ketudat Cairns, J.R. Purification of an isoflavonoid 7-O-β-apiosyl-glucoside
β-glycosidase and its substrates from Dalbergia nigrescens Kurz. Phytochemistry 66 (2005) 1880–1889. [DOI] [PMID: 16098548] |
3. |
Ahn, Y.O., Mizutani, M., Saino, H. and Sakata, K. Furcatin hydrolase from Viburnum furcatum Blume is a novel
disaccharide-specific acuminosidase in glycosyl hydrolase family 1. J. Biol. Chem. 279 (2004) 23405–23414. [DOI] [PMID: 14976214] |
|
[EC 3.2.1.161 created 2006] |
|
|
|
|
EC |
2.4.1.86 | Relevance: 88.2% |
Accepted name: |
N-acetyl-β-D-glucosaminide β-(1,3)-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-R = UDP + β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R |
|
For diagram of lactotetraosylceramide biosynthesis, click here |
Other name(s): |
B3GALT1 (gene name); uridine diphosphogalactose-acetyl-glucosaminylgalactosylglucosylceramide galactosyltransferase; GalT-4; UDP-galactose:N-acetyl-D-glucosaminyl-1,3-D-galactosyl-1,4-D-glucosylceramide β-D-galactosyltransferase; UDP-galactose:N-acetyl-D-glucosaminyl-(1→3)-D-galactosyl-(1→4)-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosylceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 3-β-D-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase; glucosaminylgalactosylglucosylceramide β-galactosyltransferase; UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase |
Systematic name: |
UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-R 3-β-D-galactosyltransferase |
Comments: |
The enzyme transfers galactose from UDP-α-D-galactose to the 3-position of substrates with a non-reducing terminal N-acetyl-β-D-glucosamine (β-GlcNAc) residue. It can act on both glycolipids and glycoproteins, generating a structure known as the type 1 histo-blood group antigen precursor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9073-46-5 |
References: |
1. |
Basu, M. and Basu, S. Enzymatic synthesis of a tetraglycosylceramide by a galactosyltransferase from rabbit bone marrow. J. Biol. Chem. 247 (1972) 1489–1495. [PMID: 4335001] |
2. |
Basu, M., Presper, K.A., Basu, S., Hoffman, L.M. and Brooks, S.E. Differential activities of glycolipid glycosyltransferases in Tay-Sachs disease: studies in cultured cells from cerebrum. Proc. Natl. Acad. Sci. USA 76 (1979) 4270–4274. [DOI] [PMID: 291963] |
3. |
Amado, M., Almeida, R., Carneiro, F., Levery, S.B., Holmes, E.H., Nomoto, M., Hollingsworth, M.A., Hassan, H., Schwientek, T., Nielsen, P.A., Bennett, E.P. and Clausen, H. A family of human β3-galactosyltransferases. Characterization of four members of a UDP-galactose:β-N-acetyl-glucosamine/β-nacetyl-galactosamine β-1,3-galactosyltransferase family. J. Biol. Chem. 273 (1998) 12770–12778. [DOI] [PMID: 9582303] |
4. |
Amado, M., Almeida, R., Schwientek, T. and Clausen, H. Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim. Biophys. Acta 1473 (1999) 35–53. [DOI] [PMID: 10580128] |
5. |
Bardoni, A., Valli, M. and Trinchera, M. Differential expression of β1,3galactosyltransferases in human colon cells derived from adenocarcinomas or normal mucosa. FEBS Lett. 451 (1999) 75–80. [DOI] [PMID: 10356986] |
|
[EC 2.4.1.86 created 1976, modified 2017] |
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|
|
|
EC |
2.4.1.175 | Relevance: 87.8% |
Accepted name: |
glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase |
Reaction: |
(1) UDP-N-acetyl-α-D-galactosamine + [protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine (2) UDP-N-acetyl-α-D-galactosamine + [protein]-3-O-(β-D-GlcA-(1→3)-[β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine = UDP + [protein]-3-O-([β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)]n+1-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine |
|
For diagram of chondroitin biosynthesis (later stages), click here |
Other name(s): |
N-acetylgalactosaminyltransferase II; UDP-N-acetyl-D-galactosamine:D-glucuronyl-N-acetyl-1,3-β-D-galactosaminylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; chondroitin synthase; glucuronyl-N-acetylgalactosaminylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase II; UDP-N-acetyl-D-galactosamine:β-D-glucuronosyl-(1→3)-N-acetyl-β-D-galactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase; UDP-N-acetyl-α-D-galactosamine:β-D-glucuronosyl-(1→3)-N-acetyl-β-D-galactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-galactosamine:[protein]-3-O-(β-D-GlcA-(1→3)-β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-serine 4-β-N-acetylgalactosaminyltransferase (configuration-inverting) |
Comments: |
Involved in the biosynthesis of chondroitin sulfate. The human form of this enzyme is a bifunctional glycosyltransferase, which also has the 3-β-glucuronosyltransferase (EC 2.4.1.226, N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase) activity required for the synthesis of the chondroitin sulfate disaccharide repeats. Similar chondroitin synthase ’co-polymerases’ can be found in Pasteurella multocida and Escherichia coli. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 96189-40-1 |
References: |
1. |
Rohrmann, K., Niemann, R. and Buddecke, E. Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate. Eur. J. Biochem. 148 (1985) 463–469. [DOI] [PMID: 3922754] |
2. |
Kitagawa, H., Uyama, T. and Sugahara, K. Molecular cloning and expression of a human chondroitin synthase. J. Biol. Chem. 276 (2001) 38721–38726. [DOI] [PMID: 11514575] |
3. |
DeAngelis, P.L. and Padgett-McCue, A.J. Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F. J. Biol. Chem. 275 (2000) 24124–24129. [DOI] [PMID: 10818104] |
4. |
Ninomiya, T., Sugiura, N., Tawada, A., Sugimoto, K., Watanabe, H. and Kimata, K. Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4. J. Biol. Chem. 277 (2002) 21567–21575. [DOI] [PMID: 11943778] |
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[EC 2.4.1.175 created 1989, modified 2002] |
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EC |
2.3.1.213 | Relevance: 87.3% |
Accepted name: |
cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) 6′′′-O-hydroxycinnamoyltransferase |
Reaction: |
1-O-(4-hydroxycinnamoyl)-β-D-glucose + cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) = β-D-glucose + cyanidin 3-O-[6-O-(6-O-4-hydroxycinnamoyl-β-D-glucosyl)-2-O-β-D-xylosyl-β-D-galactoside] |
|
For diagram of cyanidin galactoside biosynthesis, click here |
Glossary: |
1-O-(4-hydroxycinnamoyl)-β-D-glucose = 1-O-(4-coumaroyl)-β-D-glucose
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium |
Other name(s): |
1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(2"-O-xylosyl-6"-O-glucosylgalactoside) 6′′′-O-(4-hydroxycinnamoyl)transferase |
Systematic name: |
1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) 6′′′-O-(4-hydroxycinnamoyl)transferase |
Comments: |
Isolated from the plant Daucus carota (Afghan cultivar carrot). In addition to 1-O-(4-hydroxycinnamoyl)-β-D-glucose, the enzyme can use the 1-O-sinapoyl- and 1-O-feruloyl- derivatives of β-D-glucose.
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Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Gläßgen, W.E. and Seitz, H.U. Acylation of anthocyanins with hydroxycinnamic acids via 1-O-acylglucosides by protein preparations from cell cultures of Daucus carota L. Planta 186 (1992) 582–585. [PMID: 24186789] |
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[EC 2.3.1.213 created 2013] |
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|
EC |
3.2.1.64 | Relevance: 87% |
Accepted name: |
2,6-β-fructan 6-levanbiohydrolase |
Reaction: |
Hydrolysis of (2→6)-β-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(β-D-fructofuranosyl)-D-fructose, from the end of the chain |
Other name(s): |
β-2,6-fructan-6-levanbiohydrolase; 2,6-β-D-fructan 6-levanbiohydrolase; levanbiose-producing levanase; 2,6-β-D-fructan 6-β-D-fructofuranosylfructohydrolase |
Systematic name: |
(2→6)-β-D-fructofuranan 6-(β-D-fructosyl)-D-fructose-hydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-46-3 |
References: |
1. |
Avigad, G. and Zelikson, R. Cleavage of fructans to levanbiose by a specific hydrolase. Bull. Res. Counc. Isr. 11 (1963) 253–257. |
2. |
Saito, K., Kondo, K., Kojima, I., Yokota, A. and Tomita, F. Purification and characterization of 2,6-β-D-fructan 6-levanbiohydrolase from Streptomyces exfoliatus F3-2. Appl. Environ. Microbiol. 66 (2000) 252–256. [DOI] [PMID: 10618232] |
3. |
Saito, K., Oda, Y., Tomita, F. and Yokota, A. Molecular cloning of the gene for 2,6-β-D-fructan 6-levanbiohydrolase from Streptomyces exfoliatus F3-2. FEMS Microbiol. Lett. 218 (2003) 265–270. [DOI] [PMID: 12586402] |
4. |
Song, E.K., Kim, H., Sung, H.K. and Cha, J. Cloning and characterization of a levanbiohydrolase from Microbacterium laevaniformans ATCC 15953. Gene 291 (2002) 45–55. [DOI] [PMID: 12095678] |
5. |
Kang, E.J., Lee, S.O., Lee, J.D., Lee, T.H. and Lee, T.H. Purification and characterization of a levanbiose-producing levanase from Pseudomonas sp. No. 43. Biotechnol. Appl. Biochem. 29 (1999) 263–268. [PMID: 10334957] |
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[EC 3.2.1.64 created 1972, modified 2004] |
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EC |
2.4.1.206 | Relevance: 86.6% |
Accepted name: |
lactosylceramide 1,3-N-acetyl-β-D-glucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
|
For diagram of lactotetraosylceramide biosynthesis, click here |
Glossary: |
lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
lactotriosylceramide = N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
Other name(s): |
LA2 synthase; β1→3-N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-lactosylceramide β-acetylglucosaminyltransferase; lactosylceramide β-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:D-galactosyl-1,4-β-D-glucosylceramide β-1,3-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 3-β-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-N-acetylglucosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-N-acetylglucosaminyltransferase (configuration-inverting) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83682-80-8 |
References: |
1. |
Gottfries, J., Percy, A.K., Maansson, J.-E., Fredman, P., Wilkstrand, C.J., Friedman, H.S., Bigner, D.D. and Svennerholm, L. Glycolipids and glycosyltransferases in permanent cell lines established from human medulloblastomas. Biochim. Biophys. Acta 1081 (1991) 253–261. [DOI] [PMID: 1825612] |
2. |
Holmes, E.H., Hakomori, S. and Ostrander, G.K. Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed β1→3N-acetylglucosaminyltransferase. J. Biol. Chem. 262 (1987) 15649–15658. [PMID: 2960671] |
3. |
Percy, A.K., Gottfries, J., Vilbergsson, G., Maansson, J.E. and Svennerholm, J. Glycosphingolipid glycosyltransferases in human fetal brain. J. Neurochem. 56 (1991) 1461–1465. [DOI] [PMID: 1901591] |
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[EC 2.4.1.206 created 1992] |
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EC |
3.2.1.78 | Relevance: 85.9% |
Accepted name: |
mannan endo-1,4-β-mannosidase |
Reaction: |
Random hydrolysis of (1→4)-β-D-mannosidic linkages in mannans, galactomannans and glucomannans |
Other name(s): |
endo-1,4-β-mannanase; endo-β-1,4-mannase; β-mannanase B; β-1,4-mannan 4-mannanohydrolase; endo-β-mannanase; β-D-mannanase; 1,4-β-D-mannan mannanohydrolase |
Systematic name: |
4-β-D-mannan mannanohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-54-3 |
References: |
1. |
Eriksson, A.F.V. Purification and characterisation of a fungal β-mannanase. Acta Chem. Scand. 22 (1968) 1924–1934. |
2. |
Reese, E.T. β-Mannanases of fungi. Can. J. Microbiol. 11 (1965) 167–183. [PMID: 14323029] |
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[EC 3.2.1.78 created 1972] |
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EC |
3.2.1.25 | Relevance: 85.6% |
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. [DOI] [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. [PMID: 14165949] |
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[EC 3.2.1.25 created 1961] |
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EC |
3.2.1.72 | Relevance: 85.6% |
Accepted name: |
xylan 1,3-β-xylosidase |
Reaction: |
Hydrolysis of successive xylose residues from the non-reducing termini of (1→3)-β-D-xylans |
Other name(s): |
1,3-β-D-xylosidase; exo-1,3-β-xylosidase; β-1,3′-xylanase; exo-β-1,3′-xylanase; 1,3-β-D-xylan xylohydrolase |
Systematic name: |
3-β-D-xylan xylohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-50-9 |
References: |
1. |
Fukui, S., Suzuki, T., Kitahara, K. and Miwa, T. β-1,3′-Xylanase. J. Gen. Appl. Microbiol. 6 (1960) 270–282. |
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[EC 3.2.1.72 created 1972] |
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EC |
2.7.11.15 | Relevance: 85.5% |
Accepted name: |
β-adrenergic-receptor kinase |
Reaction: |
ATP + [β-adrenergic receptor] = ADP + phospho-[β-adrenergic receptor] |
Other name(s): |
ATP:β-adrenergic-receptor phosphotransferase; [β-adrenergic-receptor] kinase; β-adrenergic receptor-specific kinase; β-AR kinase; β-ARK; β-ARK 1; β-ARK 2; β-receptor kinase; GRK2; GRK3; β-adrenergic-receptor kinase (phosphorylating); β2ARK; βARK1; β-adrenoceptor kinase; β-adrenoceptor kinase 1; β-adrenoceptor kinase 2; ADRBK1; BARK1; adrenergic receptor kinase; STK15 |
Systematic name: |
ATP:[β-adrenergic receptor] phosphotransferase |
Comments: |
Requires G-protein for activation and therefore belongs to the family of G-protein-dependent receptor kinases (GRKs). Acts on the agonist-occupied form of the receptor; also phosphorylates rhodopsin, but more slowly. Does not act on casein or histones. The enzyme is inhibited by Zn2+ and digitonin but is unaffected by cyclic-AMP (cf. EC 2.7.11.14, rhodopsin kinase and EC 2.7.11.16, G-protein-coupled receptor kinase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102925-39-3 |
References: |
1. |
Benovic, J.L., Mayor, F., Jr., Staniszewski, C., Lefkowitz, R.J. and Caron, M.G. Purification and characterization of the β-adrenergic receptor kinase. J. Biol. Chem. 262 (1987) 9026–9032. [PMID: 3036840] |
2. |
Kim, C.M., Dion, S.B., Onorato, J.J. and Benovic, J.L. Expression and characterization of two β-adrenergic receptor kinase isoforms using the baculovirus expression system. Receptor 3 (1993) 39–55. [PMID: 8394172] |
3. |
Laugwitz, K.L., Kronsbein, K., Schmitt, M., Hoffmann, K., Seyfarth, M., Schomig, A. and Ungerer, M. Characterization and inhibition of β-adrenergic receptor kinase in intact myocytes. Cardiovasc Res 35 (1997) 324–333. [PMID: 9349395] |
4. |
Ferguson, S.S., Menard, L., Barak, L.S., Koch, W.J., Colapietro, A.M. and Caron, M.G. Role of phosphorylation in agonist-promoted β2-adrenergic receptor sequestration. Rescue of a sequestration-defective mutant receptor by betaARK1. J. Biol. Chem. 270 (1995) 24782–24789. [DOI] [PMID: 7559596] |
5. |
Willets, J.M., Challiss, R.A. and Nahorski, S.R. Non-visual GRKs: are we seeing the whole picture? Trends Pharmacol. Sci. 24 (2003) 626–633. [DOI] [PMID: 14654303] |
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[EC 2.7.11.15 created 1989 as EC 2.7.1.126, transferred 2005 to EC 2.7.11.15] |
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EC |
2.4.1.179 | Relevance: 85.3% |
Accepted name: |
lactosylceramide β-1,3-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + β-D-galactosyl-(1→4)-β-D-glucosyl-R = UDP + β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-R |
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For diagram of glycolipid biosynthesis, click here |
Glossary: |
lactosylceramide = β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
Other name(s): |
uridine diphosphogalactose-lactosylceramide β1→3-galactosyltransferase; UDP-galactose:D-galactosyl-1,4-β-D-glucosyl-R β-1,3-galactosyltransferase; UDP-galactose:D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase; UDP-α-D-galactose:D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase |
Systematic name: |
UDP-α-D-galactose:β-D-galactosyl-(1→4)-β-D-glucosyl-R 3-β-galactosyltransferase |
Comments: |
R may be an oligosaccharide or a glycolipid; lactose can also act as acceptor, but more slowly. Involved in the elongation of oligosaccharide chains, especially in glycolipids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 106769-64-6 |
References: |
1. |
Bailly, P., Piller, F. and Cartron, J.-P. Characterization and specific assay for a galactoside β-3-galactosyltransferase of human kidney. Eur. J. Biochem. 173 (1988) 417–422. [DOI] [PMID: 3129295] |
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[EC 2.4.1.179 created 1989] |
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EC |
3.4.19.5 | Relevance: 85.1% |
Accepted name: |
β-aspartyl-peptidase |
Reaction: |
Cleavage of a β-linked Asp residue from the N-terminus of a polypeptide |
Other name(s): |
β-aspartyl dipeptidase; β-aspartyl peptidase; β-aspartyldipeptidase |
Comments: |
Other isopeptide bonds, e.g. γ-glutamyl and β-alanyl, are not hydrolysed. A mammalian, cytosolic enzyme. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-74-7 |
References: |
1. |
Haley, E.E. β-Aspartyl peptidase from rat liver. Methods Enzymol. 19 (1970) 737–741. |
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[EC 3.4.19.5 created 1972 as EC 3.4.13.10, transferred 1992 to EC 3.4.19.5, modified 1997] |
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|
EC |
3.2.1.73 | Relevance: 85% |
Accepted name: |
licheninase |
Reaction: |
Hydrolysis of (1→4)-β-D-glucosidic linkages in β-D-glucans containing (1→3)- and (1→4)-bonds |
Other name(s): |
lichenase; β-(1→4)-D-glucan 4-glucanohydrolase; 1,3;1,4-β-glucan endohydrolase; 1,3;1,4-β-glucan 4-glucanohydrolase; 1,3-1,4-β-D-glucan 4-glucanohydrolase |
Systematic name: |
(1→3)-(1→4)-β-D-glucan 4-glucanohydrolase |
Comments: |
Acts on lichenin and cereal β-D-glucans, but not on β-D-glucans containing only 1,3- or 1,4-bonds. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-51-0 |
References: |
1. |
Barras, D.R., Moore, A.E. and Stone, B.A. Enzyme-substrate relations among β-glucan hydrolases. Adv. Chem. Ser. 95 (1969) 105–138. |
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[EC 3.2.1.73 created 1972] |
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|
EC |
3.2.1.32 | Relevance: 85% |
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. [DOI] [PMID: 16328734] |
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[EC 3.2.1.32 created 1965, modified 2011] |
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|
EC |
3.2.1.153 | Relevance: 84.9% |
Accepted name: |
fructan β-(2,1)-fructosidase |
Reaction: |
Hydrolysis of terminal, non-reducing (2→1)-linked β-D-fructofuranose residues in fructans |
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For diagram of reaction, click here |
Other name(s): |
β-(2-1)-D-fructan fructohydrolase; β-(2-1)fructan exohydrolase; inulinase; 1-FEH II; 1-fructan exohydrolase; 1-FEH w1; 1-FEH w2; β-(2-1)-linkage-specific fructan-β-fructosidase; β-(2,1)-D-fructan fructohydrolase |
Systematic name: |
β-(2→1)-D-fructan fructohydrolase |
Comments: |
Possesses one of the activities of EC 3.2.1.80, fructan β-fructosidase. While the best substrates are the inulin-type fructans, such as 1-kestose [β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside] and 1,1-nystose [β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside], some (but not all) levan-type fructans can also be hydrolysed, but more slowly [see EC 3.2.1.154, fructan β-(2,6)-fructosidase]. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1000593-08-7 |
References: |
1. |
De Roover, J., Van Laere, A., De Winter, M., Timmermans, J.W. and Van den Ende, W. Purification and properties of a second fructan exohydrolase from the roots of Cichorium intybus. Physiol. Plant. 106 (1999) 28–34. |
2. |
Van den Ende, W., Clerens, S., Vergauwen, R., Van Riet, L., Van Laere, A., Yoshida, M. and Kawakami, A. Fructan 1-exohydrolases. β-(2,1)-Trimmers during graminan biosynthesis in stems of wheat? Purification, characterization, mass mapping, and cloning of two fructan 1-exohydrolase isoforms. Plant Physiol. 131 (2003) 621–631. [DOI] [PMID: 12586886] |
|
[EC 3.2.1.153 created 2005] |
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|
|
|
EC |
3.2.1.197 | Relevance: 84.5% |
Accepted name: |
β-1,2-mannosidase |
Reaction: |
β-D-mannopyranosyl-(1→2)-β-D-mannopyranosyl-(1→2)-D-mannopyranose + H2O = β-D-mannopyranosyl-(1→2)-D-mannopyranose + α-D-mannopyranose |
Systematic name: |
β-1,2-D-mannoside mannohydrolase |
Comments: |
The enzyme, characterized from multiple bacterial species, catalyses the hydrolysis of terminal, non-reducing D-mannose residues from β-1,2-mannotriose and β-1,2-mannobiose. The mechanism involves anomeric inversion, resulting in the release of α-D-mannopyranose. Activity with β-1,2-mannotriose or higher oligosaccharides is higher than that with β-1,2-mannobiose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Cuskin, F., Basle, A., Ladeveze, S., Day, A.M., Gilbert, H.J., Davies, G.J., Potocki-Veronese, G. and Lowe, E.C. The GH130 family of mannoside phosphorylases contains glycoside hydrolases that target β-1,2-mannosidic linkages in Candida mannan. J. Biol. Chem. 290 (2015) 25023–25033. [DOI] [PMID: 26286752] |
2. |
Nihira, T., Chiku, K., Suzuki, E., Nishimoto, M., Fushinobu, S., Kitaoka, M., Ohtsubo, K. and Nakai, H. An inverting β-1,2-mannosidase belonging to glycoside hydrolase family 130 from Dyadobacter fermentans. FEBS Lett. 589 (2015) 3604–3610. [DOI] [PMID: 26476324] |
|
[EC 3.2.1.197 created 2016] |
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|
EC |
2.4.1.150 | Relevance: 84.4% |
Accepted name: |
N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-R = UDP + β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-[β-D-GlcNAc-(1→6)]-β-D-Gal-(1→4)-β-D-GlcNAc-R |
Glossary: |
β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R = type 2 precursor disaccharide |
Other name(s): |
GCNT2 (gene name); GCNT3 (gene name); IGnT; I-branching β1,6-N-acetylglucosaminyltransferase; N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-acetyllactosaminide β1→6-acetylglucosaminyltransferase; Galβ1→4GlcNAc-R β1→6 N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-1,4-N-acetyl-D-glucosaminide β-1,6-N-acetyl-D-glucosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminide 6-β-N-acetylglucosaminyltransferase (configuration-inverting) |
Comments: |
The enzyme acts on poly-N-acetyllactosamine [glycan chains of β-D-galactosyl-(1→4)-N-acetyl-D-glucosamine units connected by β(1,3) linkages] attached to proteins or lipids. It transfers a GlcNAc residue by β(1,6)-linkage to galactosyl residues close to non-reducing terminals, introducing a branching pattern known as I branching. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85638-40-0 |
References: |
1. |
Van den Eijnden, D.H., Winterwerp, H., Smeeman, P. and Schiphorst, W.E.C.M. Novikoff ascites tumor cells contain N-acetyllactosaminide β1→3 and β1→6 N-acetylglucosaminyltransferase activity. J. Biol. Chem. 258 (1983) 3435–3437. [PMID: 6219989] |
2. |
Basu, M. and Basu, S. Biosynthesis in vitro of Ii core glycosphingolipids from neolactotetraosylceramide by β 1-3- and β 1-6-N-acetylglucosaminyltransferases from mouse T-lymphoma. J. Biol. Chem. 259 (1984) 12557–12562. [PMID: 6238026] |
3. |
Piller, F., Cartron, J.P., Maranduba, A., Veyrieres, A., Leroy, Y. and Fournet, B. Biosynthesis of blood group I antigens. Identification of a UDP-GlcNAc:GlcNAc β1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase in hog gastric mucosa. J. Biol. Chem. 259 (1984) 13385–13390. [PMID: 6490658] |
4. |
Bierhuizen, M.F., Maemura, K., Kudo, S. and Fukuda, M. Genomic organization of core 2 and I branching β-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the β-1,6-N-acetylglucosaminyltransferase gene family. Glycobiology 5 (1995) 417–425. [DOI] [PMID: 7579796] |
5. |
Ujita, M., McAuliffe, J., Suzuki, M., Hindsgaul, O., Clausen, H., Fukuda, M.N. and Fukuda, M. Regulation of I-branched poly-N-acetyllactosamine synthesis. Concerted actions by I-extension enzyme, I-branching enzyme, and β1,4-galactosyltransferase I. J. Biol. Chem. 274 (1999) 9296–9304. [DOI] [PMID: 10092606] |
6. |
Yeh, J.C., Ong, E. and Fukuda, M. Molecular cloning and expression of a novel β-1,6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J. Biol. Chem. 274 (1999) 3215–3221. [DOI] [PMID: 9915862] |
|
[EC 2.4.1.150 created 1984 (EC 2.4.1.164 created 1989, incorporated 2016), modified 2017] |
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EC |
3.2.1.100 | Relevance: 84.3% |
Accepted name: |
mannan 1,4-mannobiosidase |
Reaction: |
Hydrolysis of (1→4)-β-D-mannosidic linkages in (1→4)-β-D-mannans, to remove successive mannobiose residues from the non-reducing chain ends |
Other name(s): |
1,4-β-D-mannan mannobiohydrolase; exo-β-mannanase; exo-1,4-β-mannobiohydrolase |
Systematic name: |
4-β-D-mannan mannobiohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81811-49-6 |
References: |
1. |
Araki, T. and Kitamikado, M. Purification and characterization of a novel exo-β-mannanase from Aeromonas sp. F-25. J. Biochem. (Tokyo) 91 (1982) 1181–1186. [PMID: 7096283] |
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[EC 3.2.1.100 created 1983] |
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EC |
3.2.1.58 | Relevance: 84% |
Accepted name: |
glucan 1,3-β-glucosidase |
Reaction: |
Successive hydrolysis of β-D-glucose units from the non-reducing ends of (1→3)-β-D-glucans, releasing α-glucose |
Other name(s): |
exo-1,3-β-glucosidase; β-1,3-glucan exo-hydrolase; exo (1→3)-glucanohydrolase; 1,3-β-glucan glucohydrolase |
Systematic name: |
3-β-D-glucan glucohydrolase |
Comments: |
Acts on oligosaccharides, but very slowly on laminaribiose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9073-49-8 |
References: |
1. |
Barras, D.R. and Stone, B.A. β-1,3-Glucan hydrolases from Euglena gracilis. I. The nature of the hydrolases. Biochim. Biophys. Acta 191 (1969) 329–341. [DOI] [PMID: 5354264] |
2. |
Barras, D.R. and Stone, B.A. β-1,3-Glucan hydrolases from Euglena gracilis. II. Purification and properties of the β-1,3-glucan exo-hydrolase. Biochim. Biophys. Acta 191 (1969) 342–353. [DOI] [PMID: 5354265] |
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[EC 3.2.1.58 created 1972] |
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EC |
2.4.1.201 | Relevance: 84% |
Accepted name: |
α-1,6-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] = UDP + β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-[β-D-GlcNAc-(1→4)]-[β-D-GlcNAc-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc-N-Asn-[protein] |
|
For diagram of mannosyl-glycoprotein n-acetylglucosaminyltransferases, click here |
Other name(s): |
MGAT4C (gene name); N-acetylglucosaminyltransferase VI; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase VI; uridine diphosphoacetylglucosamine-glycopeptide β-1→4-acetylglucosaminyltransferase VI; mannosyl-glycoprotein β-1,4-N-acetylglucosaminyltransferase; GnTVI; GlcNAc-T VI; UDP-N-acetyl-D-glucosamine:2,6-bis(N-acetyl-β-D-glucosaminyl)-α-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→6)-[N-acetyl-β-D-glucosaminyl-(1→2)]-α-D-mannosyl-glycoprotein 4-β-N-acetyl-D-glucosaminyltransferase (configuration-inverting) |
Comments: |
Requires a high concentration of Mn2+ for maximal activity. The enzyme, characterized from hen oviduct membranes, participates in the processing of N-glycans in the Golgi apparatus. It transfers GlcNAc in β1-4 linkage to a D-mannose residue that already has GlcNAc residues attached at positions 2 and 6 by β linkages. No homologous enzyme appears to exist in mammals. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 119699-68-2 |
References: |
1. |
Brockhausen, I., Hull, E., Hindsgaul, O., Schachter, H., Shah, R.N., Michnick, S.W. and Carver, J.P. Control of glycoprotein synthesis. Detection and characterization of a novel branching enzyme from hen oviduct, UDP-N-acetylglucosamine:GlcNAc β1-6 (GlcNAc β1-2)Man α-R (GlcNAc to Man) β-4-N-acetylglucosaminyltransferase VI. J. Biol. Chem. 264 (1989) 11211–11221. [PMID: 2525556] |
2. |
Taguchi, T., Ogawa, T., Inoue, S., Inoue, Y., Sakamoto, Y., Korekane, H. and Taniguchi, N. Purification and characterization of UDP-GlcNAc:GlcNAcβ1-6(GlcNAcβ1-2)Manα1-R [GlcNAc to Man]-β1,4-N-acetylglucosaminyltransferase VI from hen oviduct. J. Biol. Chem. 275 (2000) 32598–32602. [DOI] [PMID: 10903319] |
3. |
Sakamoto, Y., Taguchi, T., Honke, K., Korekane, H., Watanabe, H., Tano, Y., Dohmae, N., Takio, K., Horii, A. and Taniguchi, N. Molecular cloning and expression of cDNA encoding chicken UDP-N-acetyl-D-glucosamine (GlcNAc): GlcNAcβ 1-6(GlcNAcβ 1-2)- manα 1-R[GlcNAc to man]β 1,4N-acetylglucosaminyltransferase VI. J. Biol. Chem. 275 (2000) 36029–36034. [DOI] [PMID: 10962001] |
|
[EC 2.4.1.201 created 1992, modified 2001, modified 2018] |
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EC
|
1.13.12.12
|
Transferred entry: | apo-β-carotenoid-14′,13′-dioxygenase. The enzyme was misclassified and has been transferred to EC 1.13.11.67, 8-apo-β-carotenoid 14′,13′-cleaving dioxygenase
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[EC 1.13.12.12 created 2000, modified 2001, deleted 2012] |
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EC |
3.2.1.185 | Relevance: 83.9% |
Accepted name: |
non-reducing end β-L-arabinofuranosidase |
Reaction: |
β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranose + H2O = 2 β-L-arabinofuranose |
Other name(s): |
HypBA1 |
Systematic name: |
β-L-arabinofuranoside non-reducing end β-L-arabinofuranosidase |
Comments: |
The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, removes the β-L-arabinofuranose residue from the non-reducing end of multiple substrates, including β-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara2-Hyp, Ara3-Hyp, and β-L-arabinofuranosyl-(1→2)-1-O-methyl-β-L-arabinofuranose.In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. cf. EC 3.2.1.55, non-reducing end α-L-arabinofuranosidase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Fujita, K., Takashi, Y., Obuchi, E., Kitahara, K. and Suganuma, T. Characterization of a novel β-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 protein family member. J. Biol. Chem. 289 (2014) 5240–5249. [DOI] [PMID: 24385433] |
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[EC 3.2.1.185 created 2013] |
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EC |
2.4.1.275 | Relevance: 83.4% |
Accepted name: |
neolactotriaosylceramide β-1,4-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide |
|
For diagram of neolactotetraosylceramide biosynthesis, click here |
Glossary: |
N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = neolactotriaosylceramide |
Other name(s): |
β4Gal-T4; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase; lactotriaosylceramide β-1,4-galactosyltransferase (incorrect) |
Systematic name: |
UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-D-galactosyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Schwientek, T., Almeida, R., Levery, S.B., Holmes, E.H., Bennett, E. and Clausen, H. Cloning of a novel member of the UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis. J. Biol. Chem. 273 (1998) 29331–29340. [DOI] [PMID: 9792633] |
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[EC 2.4.1.275 created 2011, modified 2013] |
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EC |
3.2.1.43 | Relevance: 83.3% |
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. |
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[EC 3.2.1.43 created 1972] |
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EC |
3.2.1.154 | Relevance: 83.2% |
Accepted name: |
fructan β-(2,6)-fructosidase |
Reaction: |
Hydrolysis of terminal, non-reducing (2→6)-linked β-D-fructofuranose residues in fructans |
|
For diagram of reaction, click here |
Other name(s): |
β-(2-6)-fructan exohydrolase; levanase; 6-FEH; β-(2,6)-D-fructan fructohydrolase |
Systematic name: |
(2→6)-β-D-fructan fructohydrolase |
Comments: |
Possesses one of the activities of EC 3.2.1.80, fructan β-fructosidase. While the best substrates are the levan-type fructans such as 6-kestotriose [β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl α-D-glucopyranoside] and 6,6-kestotetraose [β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl α-D-glucopyranoside], some (but not all) inulin-type fructans can also be hydrolysed, but more slowly [cf. EC 3.2.1.153, fructan β-(2,1)-fructosidase]. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 1000597-62-5 |
References: |
1. |
Marx, S.P., Nösberger, J. and Frehner, M. Hydrolysis of fructan in grasses: A β-(2-6)-linkage specific fructan-β-fructosidase from stubble of Lolium perenne. New Phytol. 135 (1997) 279–290. |
2. |
Van den Ende, W., De Coninck, B., Clerens, S., Vergauwen, R. and Van Laere, A. Unexpected presence of fructan 6-exohydrolases (6-FEHs) in non-fructan plants: characterization, cloning, mass mapping and functional analysis of a novel 'cell-wall invertase-like' specific 6-FEH from sugar beet (Beta vulgaris L.). Plant J. 36 (2003) 697–710. [DOI] [PMID: 14617070] |
3. |
Henson, C.A. and Livingston, D.P. , III. Purification and characterization of an oat fructan exohydrolase that preferentially hydrolyzes β-2,6-fructans. Plant Physiol. 110 (1996) 639–644. [PMID: 8742337] |
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[EC 3.2.1.154 created 2005] |
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EC |
3.2.1.181 | Relevance: 83.2% |
Accepted name: |
galactan endo-β-1,3-galactanase |
Reaction: |
The enzyme specifically hydrolyses β-1,3-galactan and β-1,3-galactooligosaccharides |
Other name(s): |
endo-β-1,3-galactanase |
Systematic name: |
arabinogalactan 3-β-D-galactanohydrolase |
Comments: |
The enzyme from the fungus Flammulina velutipes (winter mushroom) hydrolyses the β(1→3) bonds found in type II plant arabinogalactans, which occur in cell walls of dicots and cereals. The enzyme is an endohydrolase, and requires at least 3 contiguous β-1,3-residues. cf. EC 3.2.1.89, arabinogalactan endo-β-1,4-galactanase and EC 3.2.1.145, galactan 1,3-β-galactosidase.
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Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kotake, T., Hirata, N., Degi, Y., Ishiguro, M., Kitazawa, K., Takata, R., Ichinose, H., Kaneko, S., Igarashi, K., Samejima, M. and Tsumuraya, Y. Endo-β-1,3-galactanase from winter mushroom Flammulina velutipes. J. Biol. Chem. 286 (2011) 27848–27854. [DOI] [PMID: 21653698] |
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[EC 3.2.1.181 created 2012] |
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EC |
2.4.1.249 | Relevance: 83.1% |
Accepted name: |
delphinidin 3′,5′-O-glucosyltransferase |
Reaction: |
2 UDP-glucose + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside = 2 UDP + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′,5′-di-O-β-D-glucoside (overall reaction) (1a) UDP-glucose + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside = UDP + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′-O-β-D-glucoside (1b) UDP-glucose + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′-O-β-D-glucoside = UDP + delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′,5′-di-O-β-D-glucoside |
|
For diagram of anthocyanidin acylglucoside biosynthesis, click here |
Glossary: |
delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′,5′-di-O-β-D-glucoside = ternatin C5 |
Other name(s): |
UDP-glucose:anthocyanin 3′,5′-O-glucosyltransferase; UA3′5’GZ |
Systematic name: |
UDP-glucose:delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside 3′-O-glucosyltransferase |
Comments: |
Ternatins are a group of polyacetylated delphinidin glucosides that confer
blue color to the petals of Clitoria ternatea (butterfly pea).
This enzyme catalyses two reactions in the biosynthesis of ternatin C5: the conversion of delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside to delphinidin 3-O-(6′′-O-malonyl)-β-D-glucoside-3′-O-β-D-glucoside, followed by the conversion of the later to ternatin C5, by transferring two glucosyl groups in a stepwise manner [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kogawa, K., Kato, N., Kazuma, K., Noda, N. and Suzuki, M. Purification and characterization of UDP-glucose: anthocyanin 3′,5′-O-glucosyltransferase from Clitoria ternatea. Planta 226 (2007) 1501–1509. [DOI] [PMID: 17668234] |
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[EC 2.4.1.249 created 2009] |
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EC |
2.4.1.38 | Relevance: 83% |
Accepted name: |
β-N-acetylglucosaminylglycopeptide β-1,4-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + N-acetyl-β-D-glucosaminylglycopeptide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminylglycopeptide |
Other name(s): |
UDP-galactose—glycoprotein galactosyltransferase; glycoprotein 4-β-galactosyl-transferase; β-N-acetyl-β1-4-galactosyltransferase; thyroid glycoprotein β-galactosyltransferase; glycoprotein β-galactosyltransferase; thyroid galactosyltransferase; uridine diphosphogalactose-glycoprotein galactosyltransferase; β-N-acetylglucosaminyl-glycopeptide β-1,4-galactosyltransferase; GalT; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide β-1,4-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase |
Systematic name: |
UDP-α-D-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase |
Comments: |
Terminal N-acetyl-β-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. High activity is shown towards such residues in branched-chain polysaccharides when these are linked by β-1,6-links to galactose residues; lower activity towards residues linked to galactose by β-1,3-links. A component of EC 2.4.1.22 (lactose synthase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37237-43-7 |
References: |
1. |
Beyer, T.A., Sadler, J.E., Rearick, J.I., Paulson, J.C. and Hill, R.L. Glucosyltransferases and their uses in assessing oligosaccharide structure and structure-function relationship. Adv. Enzymol. 52 (1981) 23–175. [PMID: 6784450] |
2. |
Blanken, W.M., Hooghwinkel, G.J.M. and van den Eijnden, D.H. Biosynthesis of blood-group I and i substances. Specificity of bovine colostrum β-N-acetyl-D-glucosaminide β1→4 galactosyltransferase. Eur. J. Biochem. 127 (1982) 547–552. [DOI] [PMID: 6816588] |
3. |
Blanken, W.M. and van den Eijnden, D.H. Biosynthesis of terminal Gal α 1→3Gal β 1→4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide α 1→3-galactosyltransferase from calf thymus. J. Biol. Chem. 260 (1985) 12927–12934. [PMID: 3932335] |
4. |
Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid galactosyltransferase. J. Biol. Chem. 243 (1968) 6529–6537. [PMID: 5726898] |
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[EC 2.4.1.38 created 1972, modified 1976, modified 1980, modified 1986] |
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