EC number:3.5.1.87
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.87 |
|---|---|
| Description: | N-carbamoyl-L-amino-acid hydrolase. |
| Alternative Name: |
N-carbamyl L-amino acid amidohydrolase. N-carbamoylase. N-carbamoyl-L-amino acid amidohydrolase. L-N-carbamoylase. L-carbamoylase. |
| Cath: | 3.30.70.360; 3.40.630.10; 3.60.110.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.87 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.87 |
| KEGG Enzyme Link: | KEGG3.5.1.87 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.87 |
| ExPASy Enzyme Link: | ExPASy3.5.1.87 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.87 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.87 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.87 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.87 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.87 |
| RHEA:17581 | an N-carbamoyl-L-2-amino acid + 2 H(+) + H2O = an L-alpha-amino acid + CO2 + NH4(+) |
| RULE(radius=1) | [*:1]-[NH;+0:2]-[C;H0;+0:3](=[*:4])-[NH2;+0:5].[H+;H0:6].[H+;H0:7].[OH2;+0:8]>>[*:1]-[NH2;+0:2].[*:4]=[C;H0;+0:3]=[O;H0;+0:8].[NH3;+0:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase M20/M25/M40 family member. | Martínez-Rodríguez S, García-Pino A, Las Heras-Vázquez FJ, Clemente-Jiménez JM, Rodríguez-Vico F, García-Ruiz JM, Loris R, Gavira JA | 2012 Nov | 22904279 |
| Molecular cloning and biochemical characterization of L-N-carbamoylase from Sinorhizobium meliloti CECT4114. | Martínez-Rodríguez S, Clemente-Jiménez JM, Rodríguez-Vico F, Las Heras-Vázquez FJ | 2005 | 16254442 |
| Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. | Altenbuchner J, Siemann-Herzberg M, Syldatk C | 2001 Dec | 11849938 |