EC 3.5.1.87 - N-carbamoyl-L-amino-acid hydrolase

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IntEnz Enzyme Nomenclature
EC 3.5.1.87

Names

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

Reaction

Cofactor

Comments:

This enzyme, along with EC 3.5.1.77 (N-carbamoyl-D-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 [3]. The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyse N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents [2]. The enzyme is inactive on derivatives of D-amino acids. In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyse formyl and acetyl derivatives to varying degrees [1,2].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050538
UniProtKB/Swiss-Prot:

References

  1. Ogawa, J., Miyake, H. and Shimizu, S.
    Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans.
    Appl. Microbiol. Biotechnol. 43: 1039-1043 (1995). [PMID: 8590654]
  2. Martínez-Rodríguez, S., Clemente-Jiménez, J.M., Rodríguez-Vico, F. and Las Heras-Vázquez, F.J.
    Molecular cloning and biochemical characterization of L-N-carbamoylase from Sinorhizobium meliloti CECT4114.
    J. Mol. Microbiol. Biotechnol. 9: 16-25 (2005). [PMID: 16254442]
  3. 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 3.5.1.87 created 2001, modified 2008]