| Type: | Family | Name: | Amidase, hydantoinase/carbamoylase |
| Description: | Hydantoinase and carbamoylasehydrolyse the amide bonds of compounds containing carbamoyl groups or hydantoin rings []. Enzymes in this subfamily are key biocatalysts for the production of optically pure amino acids from dl-5-substituted hydantoins (SSH) []. Optically pure amino acids are widely used as intermediates in the synthesis of antibiotics, antifungal agents, pesticides, and sweeteners. Of particular importance, d- p-hydroxyphenylglycine (D-HPG) can be produced from d, l-hydroxyphenly hydantoin (D,L-HPH) in a two-step reaction mediated by d-hydantoinase and N-carbamoyl- d-amino acid amidohydrolase (or carbamoylase) []. The enzymes have broad substrate specificity, and it is the first L-N-carbamoylase that hydrolyses N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents []. These enzymes are members of the broader family of amidases. | Short Name: | Amidase_hdtase/Cbmase |
