N-carbamyl-D-amino acid amidohydrolase (DCase) (DCase)

N-carbamyl-D-amino acid amidohydrolase (DCase) is a microbial enzyme, primarily found in bacteria such as Agrobacterium and Pseudomonas, that catalyzes the stereospecific hydrolysis of N-carbamyl-D-amino acids into their corresponding D-amino acids, ammonia, and carbon dioxide [11, 13]. It is a key component of the "hydantoinase process," a multi-enzyme system used for the industrial-scale production of optically pure D-amino acids [17, 24]. These D-amino acids, including D-p-hydroxyphenylglycine and D-phenylglycine, serve as essential chiral precursors for the semi-synthesis of widely used beta-lactam antibiotics such as amoxicillin and ampicillin [4, 18]. Other D-amino acids produced by this enzyme, such as D-tryptophan, are used in the synthesis of drugs like tadalafil and various therapeutic peptides [10, 18]. Structurally, DCase belongs to the nitrilase superfamily and typically functions as a homotetramer with a conserved Cys-Glu-Lys catalytic triad [11, 14]. The enzyme is highly enantioselective, acting only on the D-isomer of N-carbamyl amino acids, which makes it invaluable for producing pure enantiomers [13, 24]. Although it is not a therapeutic target in humans, it is of significant interest in biotechnology and pharmaceutical manufacturing [21, 29]. Researchers frequently use protein engineering and directed evolution to enhance its thermostability and catalytic efficiency for large-scale applications [9, 15]. It is also sensitive to thiol-reacting agents and can be inhibited by its own products, which are challenges addressed in industrial process design [13, 26].

Other names

D-carbamoylaseD-carbamoyl-amino-acid amidohydrolaseN-carbamoyl-D-amino-acid hydrolaseN-carbamoylase

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