EC number:3.5.1.14
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.14 | ||
|---|---|---|---|
| Description: | N-acyl-aliphatic-L-amino acid amidohydrolase. | ||
| Alternative Name: |
N-acyl-L-amino-acid amidohydrolase. Histozyme. Hippuricase. Dehydropeptidase II. Benzamidase. Aminoacylase I. Aminoacylase 1. Acylase I. | ||
| Prosite: | PDOC00613; | ||
| PDB: |
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| Cath: | 3.30.70.1640; 3.30.70.360; 3.40.630.10; 2.20.25.160; |
3D structure
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.14 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.14 |
| KEGG Enzyme Link: | KEGG3.5.1.14 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.14 |
| ExPASy Enzyme Link: | ExPASy3.5.1.14 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.14 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.14 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.14 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.14 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.14 |
| RHEA:36855 | an N-acetyl-L-cysteine-S-conjugate + H2O = acetate + an S-substituted L-cysteine |
| RULE(radius=1) | [*:1]-[NH;+0:2]-[C;H0;+0:3](=[*:4])-[*:5].[OH2;+0:6]>>[*:1]-[NH2;+0:2].[*:4]=[C;H0;+0:3](-[*:5])-[OH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Aminoacylase I from porcine kidney: identification and characterization of two major protein domains. | Palm GJ, Röhm KH | 1995 May | 7662111 |
| Aminoacylase I from hog kidney: anion effects and the pH dependence of kinetic parameters. | Henseling J, Röhm KH | 1988 Apr 15 | 3355856 |
| Nuclear magnetic relaxation studies of the role of the metal ion in Mn2(+)-substituted aminoacylase I. | Heese D, Berger S, Röhm KH | 1990 Feb 22 | 2318199 |
| Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family. | Lindner HA, Lunin VV, Alary A, Hecker R, Cygler M, Ménard R | 2003 Nov 7 | 12933810 |
| The distribution of aminoacylase I among mammalian species and localization of the enzyme in porcine kidney. | Lindner H, Höpfner S, Täfler-Naumann M, Miko M, Konrad L, Röhm KH | 2000 Feb | 10727768 |
| Inhibition of aminoacylase 3 protects rat brain cortex neuronal cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and 4-hydroxy-2-nonenal. | Tsirulnikov K, Abuladze N, Bragin A, Faull K, Cascio D, Damoiseaux R, Schibler MJ, Pushkin A | 2012 Sep 15 | 22819785 |
| Structures of aminoacylase 3 in complex with acetylated substrates. | Hsieh JM, Tsirulnikov K, Sawaya MR, Magilnick N, Abuladze N, Kurtz I, Abramson J, Pushkin A | 2010 Oct 19 | 20921362 |
| Mouse aminoacylase 3: a metalloenzyme activated by cobalt and nickel. | Tsirulnikov K, Abuladze N, Newman D, Ryazantsev S, Wolak T, Magilnick N, Koag MC, Kurtz I, Pushkin A | 2009 Jul | 19362172 |
| Specificity of aminoacylase III-mediated deacetylation of mercapturic acids. | Newman D, Abuladze N, Scholz K, Dekant W, Tsuprun V, Ryazantsev S, Bondar G, Sassani P, Kurtz I, Pushkin A | 2007 Jan | 17012540 |
| Structural characterization, tissue distribution, and functional expression of murine aminoacylase III. | Pushkin A, Carpenito G, Abuladze N, Newman D, Tsuprun V, Ryazantsev S, Motemoturu S, Sassani P, Solovieva N, Dukkipati R, Kurtz I | 2004 Apr | 14656720 |
| RHEA:15565 | an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[NH2;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Acylase I-catalyzed deacetylation of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines. | Uttamsingh V, Keller DA, Anders MW | 1998 Jul | 9671543 |
| Aminoacylase I from porcine kidney: identification and characterization of two major protein domains. | Palm GJ, Röhm KH | 1995 May | 7662111 |
| Aminoacylase I from hog kidney: anion effects and the pH dependence of kinetic parameters. | Henseling J, Röhm KH | 1988 Apr 15 | 3355856 |
| Nuclear magnetic relaxation studies of the role of the metal ion in Mn2(+)-substituted aminoacylase I. | Heese D, Berger S, Röhm KH | 1990 Feb 22 | 2318199 |
| Roles of dimerization domain residues in binding and catalysis by aminoacylase-1. | Lindner HA, Alary A, Boju LI, Sulea T, Ménard R | 2005 Dec 6 | 16313167 |
| Site-directed mutagenesis and molecular modelling studies show the role of Asp82 and cysteines in rat acylase 1, a member of the M20 family. | Herga S, Brutus A, Vitale RM, Miche H, Perrier J, Puigserver A, Scaloni A, Giardina T | 2005 May 6 | 15796916 |
| Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family. | Lindner HA, Lunin VV, Alary A, Hecker R, Cygler M, Ménard R | 2003 Nov 7 | 12933810 |
| The distribution of aminoacylase I among mammalian species and localization of the enzyme in porcine kidney. | Lindner H, Höpfner S, Täfler-Naumann M, Miko M, Konrad L, Röhm KH | 2000 Feb | 10727768 |