KEGG   ENZYME: 3.5.1.77Help
Entry
EC 3.5.1.77                 Enzyme                                 

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
BRITE hierarchy
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)
Substrate
N-carbamoyl-D-amino acid [CPD:C05226];
H2O [CPD:C00001]
Product
D-amino acid [CPD:C00405];
NH3 [CPD:C00014];
CO2 [CPD:C00011]
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.
History
EC 3.5.1.77 created 1999, modified 2008
Orthology
K01459  
Genes
RFR: 
RET: 
BJA: 
BRA: 
BBT: 
RPE: 
NWI: 
NHA: 
RDE: 
Taxonomy
Reference
1  [PMID:8462543]
  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.
Reference
2  [PMID:11849938]
  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

DBGET integrated database retrieval system