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Information on EC - N-carbamoyl-L-amino-acid hydrolase

for references in articles please use BRENDA:EC3.5.1.87
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IUBMB 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 . 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 . 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].
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The enzyme appears in viruses and cellular organisms
l-n-carbamoylase, bslcar, l-carbamoylase, n-carbamyl-l-amino acid amidohydrolase, l-methionine-n-carbamoylase, n-carbamoyl-l-cysteine amidohydrolase, ncc amidohydrolase, l-ncc amidohydrolase, n-carbamoyl-l-amino acid amidohydrolase, smlcar, more
an N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = an L-2-amino acid + NH3 + CO2
show the reaction diagram