| EC |
3.5.1.77 |
| Accepted name: |
N-carbamoyl-D-amino-acid hydrolase |
| Reaction: |
an N-carbamoyl-D-amino acid + H2O = a D-amino acid + NH3 + CO2 |
| Other name(s): |
D-N-carbamoylase; N-carbamoylase (ambiguous); N-carbamoyl-D-amino acid hydrolase |
| Systematic name: |
N-carbamoyl-D-amino-acid amidohydrolase |
| Comments: |
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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 71768-08-6 |
| References: |
| 1. |
Ogawa, J., Shimizu, S., Yamada, H. N-Carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c; purification and characterization. Eur. J. Biochem. 212 (1993) 685–691. [DOI] [PMID: 8462543] |
| 2. |
Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559–563. [DOI] [PMID: 11849938] |
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| [EC 3.5.1.77 created 1999, modified 2008] |
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