EC 3.5.1.77 - N-carbamoyl-D-amino-acid hydrolase

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IntEnz Enzyme Nomenclature
EC 3.5.1.77

Names

Accepted name:
N-carbamoyl-D-amino-acid hydrolase
Other names:
D-N-carbamoylase
N-carbamoylase [ambiguous]
N-carbamoyl-D-amino acid hydrolase
Systematic name:
N-carbamoyl-D-amino-acid amidohydrolase

Reaction

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 N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropionate, which are substrates for other amidohydrolases.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047417
CAS Registry Number: 71768-08-6
UniProtKB/Swiss-Prot:

References

  1. Ogawa, J., Shimizu, S. and Yamada, H.
    N-Carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c; purification and characterization.
    Eur. J. Biochem. 212 : 685-691 (1993). [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 : 559-563 (2001). [PMID: 11849938]

[EC 3.5.1.77 created 1999, modified 2008]