EC |
2.3.1.80 |
Accepted name: |
cysteine-S-conjugate N-acetyltransferase |
Reaction: |
acetyl-CoA + an L-cysteine-S-conjugate = CoA + an N-acetyl-L-cysteine-S-conjugate |
Glossary: |
N-acetyl-L-cysteine-S-conjugate = mercapturic acid |
Systematic name: |
acetyl-CoA:S-substituted L-cysteine N-acetyltransferase |
Comments: |
S-Benzyl-L-cysteine and, in decreasing order of activity, S-butyl-L-cysteine, S-propyl-L-cysteine, O-benzyl-L-serine and S-ethyl-L-cysteine, can act as acceptors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81725-80-6 |
References: |
1. |
Duffel, M.W. and Jakoby, W.B. Cysteine S-conjugate N-acetyltransferase from rat kidney microsomes. Mol. Pharmacol. 21 (1982) 444–448. [PMID: 6892478] |
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[EC 2.3.1.80 created 1984] |
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EC |
3.5.1.14 |
Accepted name: |
N-acyl-aliphatic-L-amino acid amidohydrolase |
Reaction: |
(1) an N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate (2) an N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate |
Glossary: |
N-acetyl-L-cysteine-S-conjugate = mercapturic acid |
Other name(s): |
aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase |
Systematic name: |
N-acyl-aliphatic-L-amino acid amidohydrolase (carboxylate-forming) |
Comments: |
Contains Zn2+. The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-α-amino acids. Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.15, aspartoacylase and EC 3.5.1.114, N-acyl-aromatic-L-amino acid amidohydrolase. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9012-37-7 |
References: |
1. |
Birnbaum, S.M., Levintow, L., Kingsley, R.B. and Greenstein, J.P. Specificity of amino acid acylases. J. Biol. Chem. 194 (1952) 455–470. [PMID: 14927637] |
2. |
Fones, W.S. and Lee, M. Hydrolysis of N-acyl derivatives of alanine and phenylalanine by acylase I and carboxypeptidase. J. Biol. Chem. 201 (1953) 847–856. [PMID: 13061423] |
3. |
Henseling, J. and Rohm, K.H. Aminoacylase I from hog kidney: anion effects and the pH dependence of kinetic parameters. Biochim. Biophys. Acta 959 (1988) 370–377. [DOI] [PMID: 3355856] |
4. |
Heese, D., Berger, S. and Rohm, K.H. Nuclear magnetic relaxation studies of the role of the metal ion in Mn2+-substituted aminoacylase I. Eur. J. Biochem. 188 (1990) 175–180. [DOI] [PMID: 2318199] |
5. |
Palm, G.J. and Rohm, K.H. Aminoacylase I from porcine kidney: identification and characterization of two major protein domains. J. Protein Chem. 14 (1995) 233–240. [PMID: 7662111] |
6. |
Uttamsingh, V., Keller, D.A. and Anders, M.W. Acylase I-catalyzed deacetylation of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines. Chem. Res. Toxicol. 11 (1998) 800–809. [DOI] [PMID: 9671543] |
7. |
Lindner, H., Hopfner, S., Tafler-Naumann, M., Miko, M., Konrad, L. and Rohm, K.H. The distribution of aminoacylase I among mammalian species and localization of the enzyme in porcine kidney. Biochimie 82 (2000) 129–137. [DOI] [PMID: 10727768] |
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[EC 3.5.1.14 created 1965, modified 2013] |
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EC |
3.5.1.114 |
Accepted name: |
N-acyl-aromatic-L-amino acid amidohydrolase |
Reaction: |
(1) an N-acyl-aromatic-L-amino acid + H2O = an aromatic-L-amino acid + a carboxylate (2) an N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate |
Glossary: |
N-acetyl-L-cysteine-S-conjugate = mercapturic acid |
Other name(s): |
aminoacylase 3; aminoacylase III; ACY3 (gene name) |
Systematic name: |
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) |
Comments: |
This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It preferentially deacetylates Nα-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase. The enzyme is significantly activated by Co2+ and Ni2+ [3]. Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase and EC 3.5.1.15, aspartoacylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Pushkin, A., Carpenito, G., Abuladze, N., Newman, D., Tsuprun, V., Ryazantsev, S., Motemoturu, S., Sassani, P., Solovieva, N., Dukkipati, R. and Kurtz, I. Structural characterization, tissue distribution, and functional expression of murine aminoacylase III. Am. J. Physiol. Cell Physiol. 286 (2004) C848–C856. [DOI] [PMID: 14656720] |
2. |
Newman, D., Abuladze, N., Scholz, K., Dekant, W., Tsuprun, V., Ryazantsev, S., Bondar, G., Sassani, P., Kurtz, I. and Pushkin, A. Specificity of aminoacylase III-mediated deacetylation of mercapturic acids. Drug Metab. Dispos. 35 (2007) 43–50. [DOI] [PMID: 17012540] |
3. |
Tsirulnikov, K., Abuladze, N., Newman, D., Ryazantsev, S., Wolak, T., Magilnick, N., Koag, M.C., Kurtz, I. and Pushkin, A. Mouse aminoacylase 3: a metalloenzyme activated by cobalt and nickel. Biochim. Biophys. Acta 1794 (2009) 1049–1057. [DOI] [PMID: 19362172] |
4. |
Hsieh, J.M., Tsirulnikov, K., Sawaya, M.R., Magilnick, N., Abuladze, N., Kurtz, I., Abramson, J. and Pushkin, A. Structures of aminoacylase 3 in complex with acetylated substrates. Proc. Natl. Acad. Sci. USA 107 (2010) 17962–17967. [DOI] [PMID: 20921362] |
5. |
Tsirulnikov, K., Abuladze, N., Bragin, A., Faull, K., Cascio, D., Damoiseaux, R., Schibler, M.J. and Pushkin, A. Inhibition of aminoacylase 3 protects rat brain cortex neuronal cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and 4-hydroxy-2-nonenal. Toxicol. Appl. Pharmacol. 263 (2012) 303–314. [DOI] [PMID: 22819785] |
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[EC 3.5.1.114 created 2013] |
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