D-amino acid amidase (DAA)

D-amino acid amidase is a stereospecific enzyme that catalyzes the hydrolysis of D-amino acid amides into their corresponding D-amino acids and ammonia. Primarily identified in bacterial species such as Ochrobactrum anthropi and Delftia acidovorans, this enzyme plays a significant role in the metabolism of D-enantiomers, which are critical components of the bacterial peptidoglycan cell wall [11, 17, 26]. While it is not a recognized therapeutic target for any currently approved drugs, D-amino acid amidase is highly valued in the biotechnology industry for the production of enantiopure D-amino acids [2, 10, 24]. These D-amino acids serve as essential chiral building blocks for the synthesis of various pharmaceuticals, including semi-synthetic beta-lactam antibiotics, the antidiabetic drug nateglinide, and several neuroprotective compounds [10, 22, 23]. Structurally, the enzyme belongs to the penicillin-recognizing protein family and shares conserved motifs with penicillin-binding proteins and DD-peptidases, suggesting a potential, though currently experimental, role as a target for novel antimicrobial agents [20, 22].

Other names

D-amidaseD-amino acid amide hydrolaseD-stereospecific amino acid amidaseD-amino acid amidohydrolaseD-aminoacylaseN-acyl-D-amino-acid deacylase

Catalyzes the hydrolysis of the C-N bond in D-amino acid amides to produce D-amino acids and ammonia.