N-carbamoyl-L-amino-acid hydrolase;
N-carbamyl L-amino acid amidohydrolase;
N-carbamoyl-L-amino acid amidohydrolase;
L-N-carbamoylase;
N-carbamoylase (ambiguous)

Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides

N-carbamoyl-L-amino-acid amidohydrolase

an N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = an L-2-amino acid + NH3 + CO2 [RN:R05782]

R05782;
(other) R00254

N-carbamoyl-L-2-amino acid [CPD:C11529];
H2O [CPD:C00001]

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].

1  [PMID:8590654]

Ogawa J, Miyake H, Shimizu S.

Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans.

Appl. Microbiol. Biotechnol. 43 (1995) 1039-43.

Alcaligenes xylosoxidans

2  [PMID:16254442]

Martinez-Rodriguez S, Clemente-Jimenez JM, Rodriguez-Vico F, Las Heras-Vazquez FJ

Molecular cloning and biochemical characterization of L-N-carbamoylase from Sinorhizobium meliloti CECT4114.

J. Mol. Microbiol. Biotechnol. 9 (2005) 16-25.

Sinorhizobium meliloti [GN:sme]

3  [PMID:11849938]

Altenbuchner J, Siemann-Herzberg M, Syldatk C

Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids.

Curr. Opin. Biotechnol. 12 (2001) 559-63.

Arthrobacter aurescens [GN:aau]