ENZYME entry: EC 3.5.1.87
| Accepted Name |
| N-carbamoyl-L-amino-acid hydrolase.
|
| Alternative Name(s) |
| L-carbamoylase. |
| L-N-carbamoylase. |
| N-carbamoyl-L-amino acid amidohydrolase. |
| N-carbamoylase. |
| N-carbamyl L-amino acid amidohydrolase. |
| Reaction catalysed |
| N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H(2)O <=> L-2-amino acid + NH(3) + CO(2) |
| Cofactor(s) |
| Cobalt or nickel or manganese.
|
| Comment(s) |
- This enzyme, along with EC 3.5.1.77, EC 5.1.99.5 and EC 3.5.2.2,
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 hydrolyze 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
hydrolyze formyl and acetyl derivatives to varying degrees.
|
| Cross-references |
| BRENDA | 3.5.1.87 |
| EC2PDB | 3.5.1.87 |
| ExplorEnz | 3.5.1.87 |
| PRIAM enzyme-specific profiles | 3.5.1.87 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.5.1.87 |
| IUBMB Enzyme Nomenclature | 3.5.1.87 |
| IntEnz | 3.5.1.87 |
| MEDLINE | Find literature relating to 3.5.1.87 |
| MetaCyc | 3.5.1.87 |
| UniProtKB/Swiss-Prot |
|
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