| Entry |
|
| Name |
N-carbamoyl-D-amino-acid hydrolase;
D-N-carbamoylase;
N-carbamoylase (ambiguous);
N-carbamoyl-D-amino acid hydrolase
|
| Class |
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
 |
| Sysname |
N-carbamoyl-D-amino-acid amidohydrolase
|
| Reaction(IUBMB) |
an N-carbamoyl-D-amino acid + H2O = a D-amino acid + NH3 + CO2 [RN: R02190]
|
| Reaction(KEGG) |
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| Substrate |
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| Product |
|
| Comment |
This enzyme, along with EC 3.5.1.87 (N-carbamoyl-L-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [2]. It has strict stereospecificity for N-carbamoyl-D-amino acids and does not act upon the corresponding L-amino acids or on the N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropanoate, which are substrates for other amidohydrolases.
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| Orthology |
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| Genes |
RFR: | | HPA: | | RET: | | BJA: | | BRA: | | BBT: | | RPE: | | NWI: | | NHA: | | RDE: | |
 |
| Reference |
|
| Authors |
Ogawa J, Shimizu S, Yamada H. |
| Title |
N-carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c purification and characterization. |
| Journal |
Eur. J. Biochem. 212 (1993) 685-91. |
| Organism |
Comamonas sp. |
| Reference |
|
| Authors |
Altenbuchner J, Siemann-Herzberg M, Syldatk C |
| Title |
Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. |
| Journal |
Curr. Opin. Biotechnol. 12 (2001) 559-63. |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 71768-08-6 |