The Enzyme Database

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Accepted name: N-carbamoyl-L-amino-acid hydrolase
Reaction: an N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = an L-2-amino acid + NH3 + CO2
Other name(s): 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
Comments: This enzyme, along with EC (N-carbamoyl-D-amino-acid hydrolase), EC (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: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
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 (1995) 1039–1043. [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 (2005) 16–25. [DOI] [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 (2001) 559–563. [DOI] [PMID: 11849938]
[EC created 2001, modified 2008]

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