N-carbamoyl-D-amino acid amidohydrolase (D-carbamoylase)

N-carbamoyl-D-amino acid amidohydrolase, commonly known as D-carbamoylase, is an enzyme that catalyzes the hydrolysis of N-carbamoyl-D-amino acids into their corresponding D-amino acids, ammonia, and carbon dioxide [PubMed: 12644501]. This enzyme is primarily found in microorganisms such as Agrobacterium, Pseudomonas, and Arthrobacter species, where it plays a role in the metabolism of D-amino acids [PubMed: 11557313]. In humans, the functional homolog is beta-ureidopropionase (UPB1), which is involved in the final step of the pyrimidine degradation pathway, converting N-carbamoyl-beta-alanine to beta-alanine [UniProt: Q9UBR1]. D-carbamoylase is of significant industrial importance as a biocatalyst in the production of enantiopure D-amino acids, which are essential intermediates for the synthesis of semi-synthetic beta-lactam antibiotics like amoxicillin and ampicillin [PubMed: 15590410]. While it is not a traditional therapeutic target for drug inhibition, genetic mutations in the human homolog UPB1 lead to beta-ureidopropionase deficiency, a rare metabolic disorder associated with neurological symptoms such as seizures and developmental delay [NCBI: NBK1116]. The enzyme's high stereoselectivity and efficiency make it a key tool in green chemistry and pharmaceutical manufacturing rather than a target for pharmacological intervention.

Other names

D-amino acid carbamoylaseN-carbamoyl-D-amino-acid hydrolaseBeta-ureidopropionase

Catalyzes the hydrolysis of N-carbamoyl-D-amino acids to their corresponding D-amino acids, carbon dioxide, and ammonia via a nucleophilic attack by a catalytic cysteine residue [PubMed: 11557313].