InterPro domain: IPR010158

L-carbamoylases (N-carbamoyl-L-amino-acid amidohydrolases) hydrolyze the amide bond of the carbamoyl group in L-N-carbamoyl-amino acids [ 1 ]. They are important industrial enzymes widely used for the production of optically pure amino acids due to their stereospecificity. Furthermore, their substrate promiscuity allows their use in different multienzymatic processes [ 2 , 3 ].

Also included in this family is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism [ 4 ], and yeast N-carbamyl-beta-alanine amidohydrolase (betaAS, beta-alanine synthase) [ 5 , 6 ].

These enzymes are members of the broader family of amidases.

1. Molecular cloning and biochemical characterization of L-N-carbamoylase from Sinorhizobium meliloti CECT4114. J. Mol. Microbiol. Biotechnol. 9, 16-25
2. Evaluation of substrate promiscuity of an L-carbamoyl amino acid amidohydrolase from Geobacillus stearothermophilus CECT43. Biotechnol. Prog. 26, 954-9
3. Carbamoylases: characteristics and applications in biotechnological processes. Appl. Microbiol. Biotechnol. 85, 441-58
4. Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics. J. Mol. Biol. 368, 450-63
5. Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements. J. Biol. Chem. 282, 36037-47
6. Yeast beta-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases. J. Biol. Chem. 278, 51851-62