ExplorEnz: EC 3.5.1.2*

Your query returned 11 entries. Printable version

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. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 285–300.

[EC 3.5.1.2 created 1961]

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]

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]

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]

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, PDB, 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]

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]

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)]

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)]

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]

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)]

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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, 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]