The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 3.5.1.2     
Accepted name: glutaminase
Reaction: L-glutamine + H2O = L-glutamate + NH3
Other name(s): glutaminase I; L-glutaminase; glutamine aminohydrolase
Systematic name: L-glutamine amidohydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-47-2
References:
1.  Kung, H.-F. and Wagner, C. γ-Glutamylmethylamide. A new intermediate in the metabolism of methylamine. J. Biol. Chem. 244 (1969) 4136–4140. [PMID: 5800436]
2.  Roberts, E. Glutaminase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 285–300.
[EC 3.5.1.2 created 1961]
 
 
EC 3.5.1.20     
Accepted name: citrullinase
Reaction: L-citrulline + H2O = L-ornithine + CO2 + NH3
Other name(s): citrulline ureidase; citrulline hydrolase; L-citrulline 5-N-carbamoyldihydrolase
Systematic name: L-citrulline N5-carbamoyldihydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 59088-17-4
References:
1.  Hill, D.L. and Chambers, P. The biosynthesis of proline by Tetrahymena pyriformis. Biochim. Biophys. Acta 148 (1967) 435–447. [DOI] [PMID: 6075416]
[EC 3.5.1.20 created 1972]
 
 
EC 3.5.1.21     
Accepted name: N-acetyl-β-alanine deacetylase
Reaction: N-acetyl-β-alanine + H2O = acetate + β-alanine
Systematic name: N-acetyl-β-alanine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-04-6
References:
1.  Fujimoto, D., Koyama, T. and Tamiya, N. N-Acetyl-β-alanine deacetylase in hog kidney. Biochim. Biophys. Acta 167 (1968) 407–413.
[EC 3.5.1.21 created 1972]
 
 
EC 3.5.1.22     
Accepted name: pantothenase
Reaction: (R)-pantothenate + H2O = (R)-pantoate + β-alanine
For diagram of pantothenate catabolism, click here
Other name(s): pantothenate hydrolase; pantothenate amidohydrolase
Systematic name: (R)-pantothenate amidohydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9076-90-8
References:
1.  Nurmikko, V., Salo, E., Hakola, H., Makinen, K. and Snell, E.E. The bacterial degradation of pantothenic acid. II. Pantothenate hydrolase. Biochemistry 5 (1966) 399–402. [PMID: 5940928]
[EC 3.5.1.22 created 1972]
 
 
EC 3.5.1.23     
Accepted name: ceramidase
Reaction: a ceramide + H2O = a carboxylate + sphingosine
Glossary: a ceramide = an N-acylsphingosine
Other name(s): acylsphingosine deacylase; glycosphingolipid ceramide deacylase
Systematic name: N-acylsphingosine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-06-8
References:
1.  Nilsson, A. The presence of spingomyelin- and ceramide-cleaving enzymes in the small intestinal tract. Biochim. Biophys. Acta 176 (1969) 339–347. [DOI] [PMID: 5775951]
2.  Yavin, E. and Gatt, S. Enzymatic hydrolysis of sphingolipids. 8. Further purification and properties of rat brain ceramidase. Biochemistry 8 (1969) 1692–1698. [PMID: 5805303]
[EC 3.5.1.23 created 1972, modified 1990]
 
 
EC 3.5.1.24     
Accepted name: choloylglycine hydrolase
Reaction: glycocholate + H2O = cholate + glycine
For diagram of cholic acid conjugates biosynthesis, click here
Glossary: glycocholate = N-(3α,7α,12α-trihydroxy-5β-cholan-24-oyl)glycine
cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate
Other name(s): glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase
Systematic name: glycocholate amidohydrolase
Comments: Also acts on the 3α,12α-dihydroxy-derivative, and on choloyl-taurine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-07-9
References:
1.  Nair, P.P., Gordon, M. and Reback, J. The enzymatic cleavage of the carbon-nitrogen bond in 3α,7α,12α-trihydroxy-5-β-cholan-24-oylglycine. J. Biol. Chem. 242 (1967) 7–11. [PMID: 6016335]
2.  Stellwag, E.J. and Hylemon, P.B. Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis. Biochim. Biophys. Acta 452 (1976) 165–176. [DOI] [PMID: 10993]
[EC 3.5.1.24 created 1972]
 
 
EC 3.5.1.25     
Accepted name: N-acetylglucosamine-6-phosphate deacetylase
Reaction: N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate
For diagram of the biosynthesis of UDP-N-acetylglucosamine, click here
Other name(s): acetylglucosamine phosphate deacetylase; acetylaminodeoxyglucosephosphate acetylhydrolase; 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase
Systematic name: N-acetyl-D-glucosamine-6-phosphate amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-50-3
References:
1.  White, R.J. and Pasternak, C.A. The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli. Biochem. J. 105 (1967) 121–125. [PMID: 4861885]
2.  Yamano, N., Matsushita, Y., Kamada, Y., Fujishima, S., Arita, M. Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from Vibrio cholerae non-O1. Biosci. Biotechnol. Biochem. 60 (1996) 1320–1323. [DOI] [PMID: 8987551]
[EC 3.5.1.25 created 1972 (EC 3.5.1.80 created 1999, incorporated 2002)]
 
 
EC 3.5.1.26     
Accepted name: N4-(β-N-acetylglucosaminyl)-L-asparaginase
Reaction: N4-(β-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-β-D-glucosaminylamine + L-aspartate
Other name(s): aspartylglucosylamine deaspartylase; aspartylglucosylaminase; aspartylglucosaminidase; aspartylglycosylamine amidohydrolase; N-aspartyl-β-glucosaminidase; glucosylamidase; β-aspartylglucosylamine amidohydrolase; 4-N-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
Systematic name: N4-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
Comments: Acts only on asparagine-oligosaccharides containing one amino acid, i.e., the asparagine has free α-amino and α-carboxyl groups [cf. EC 3.5.1.52, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-24-5
References:
1.  Kohno, M. and Yamashina, I. Purification and properties of 4-L-aspartylglycosylamine amidohydrolase from hog kidney. Biochim. Biophys. Acta 258 (1972) 600–617. [DOI] [PMID: 5010303]
2.  Mahadevan, S. and Tappel, A.L. β-Aspartylglucosylamine amido hydrolase of rat liver and kidney. J. Biol. Chem. 242 (1967) 4568–4576. [PMID: 6061403]
3.  Tarentino, A.L. and Maley, F. The purification and properties of a β-aspartyl N-acetylglucosylamine amidohydrolase from hen oviduct. Arch. Biochem. Biophys. 130 (1969) 295–303. [PMID: 5778645]
[EC 3.5.1.26 created 1972 (EC 3.5.1.37 created 1972, incorporated 1976)]
 
 
EC 3.5.1.27      
Deleted entry: N-formylmethionylaminoacyl-tRNA deformylase. The activity is covered by EC 3.5.1.88, peptide deformylase
[EC 3.5.1.27 created 1972, deleted 2014]
 
 
EC 3.5.1.28     
Accepted name: N-acetylmuramoyl-L-alanine amidase
Reaction: Hydrolyses the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
Other name(s): acetylmuramyl-L-alanine amidase; N-acetylmuramyl-L-alanine amidase; N-acylmuramyl-L-alanine amidase; acetylmuramoyl-alanine amidase; N-acetylmuramic acid L-alanine amidase; acetylmuramyl-alanine amidase; N-acetylmuramylalanine amidase; murein hydrolase; N-acetylmuramoyl-L-alanine amidase type I; N-acetylmuramoyl-L-alanine amidase type II
Systematic name: peptidoglycan amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-25-6
References:
1.  Ghuysen, J.-M., Dierickx, L., Coyette, J., Leyh-Bouille, M., Guinand, M. and Campbell, J.N. An improved technique for the preparation of Streptomyces peptidases and N-acetylmuramyl-L-alanine amidase active on bacterial wall peptidoglycans. Biochemistry 8 (1969) 213–222. [PMID: 5777325]
2.  Herbold, D.R. and Glaser, L. Interaction of N-acetylmuramic acid L-alanine amidase with cell wall polymers. J Biol Chem 250 (1975) 7231–7238. [PMID: 809432]
3.  Herbold, D.R. and Glaser, L. Bacillus subtilis N-acetylmuramic acid L-alanine amidase. J. Biol. Chem. 250 (1975) 1676–1682. [PMID: 803507]
4.  Ward, J.B., Curtis, C.A.M., Taylor, C. and Buxton, R.S. Purification and characterization of two phage PBSX-induced lytic enzymes of Bacillus subtilis 168: an N-acetylmuramoyl-L-alanine amidase and an N-acetylmuramidase. J. Gen. Microbiol. 128 (1982) 1171–1178. [DOI] [PMID: 6126517]
[EC 3.5.1.28 created 1972 (EC 3.4.19.10 created 1992, incorporated 1997)]
 
 
EC 3.5.1.29     
Accepted name: 2-(acetamidomethylene)succinate hydrolase
Reaction: 2-(acetamidomethylene)succinate + 2 H2O = acetate + succinate semialdehyde + NH3 + CO2
Other name(s): α-(N-acetylaminomethylene)succinic acid hydrolase
Systematic name: 2-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)
Comments: Involved in the degradation of pyridoxin in Pseudomonas.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37289-09-1
References:
1.  Huynh, M.S. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of two N-acetylamidohydrolases. J. Biol. Chem. 260 (1985) 2379–2383. [PMID: 3972793]
2.  Nyns, E.J., Zach, D. and Snell, E.E. The bacterial oxidation of vitamin B6. 8. Enzymatic breakdown of α-(N-acetylaminomethylene) succinic acid. J. Biol. Chem. 244 (1969) 2601–2605. [PMID: 5769993]
[EC 3.5.1.29 created 1972]
 
 


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