Characterization of human d-amino acid oxidase

• Published in: FEBS letters Vol. 580; no. 9; pp. 2358 - 2364
• Main Authors: Molla, Gianluca, Sacchi, Silvia, Bernasconi, Mariagrazia, Pilone, Mirella S., Fukui, Kiyoshi, Pollegioni, Loredano
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 17.04.2006
• Subjects: Brain - enzymology; Coenzymes - chemistry; Coenzymes - metabolism; d-AA; d-amino acid; d-amino acid oxidase; d-amino acid oxidase from human; d-amino acid oxidase from pig kidney; d-amino acid oxidase from Rhodotorula gracilis; D-Amino-Acid Oxidase - chemistry; D-Amino-Acid Oxidase - metabolism; DAAO; Dimerization; Enzyme Activators - chemistry; Enzyme Activators - metabolism; Escherichia coli; Flavoprotein; hDAAO; Humans; imino acid; Kinetics; Neurotransmission; pkDAAO; Protein Binding; Protein Structure, Quaternary; Receptors, N-Methyl-D-Aspartate - metabolism; RgDAAO; Schizophrenia; Schizophrenia - enzymology; Serine - chemistry; Serine - metabolism; DAAO; pkDAAO; d-AA; RgDAAO; IA; Schizophrenia; hDAAO; d-amino acid; Flavoprotein; Neurotransmission
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2006.03.045

d-Amino acid oxidase (DAAO) has been proposed to be involved in the oxidation of d-serine, an allosteric activator of the NMDA-type glutamate receptor in the brain, and to be associated with the onset of schizophrenia. The recombinant human DAAO was expressed in Escherichia coli and was isolated as an active homodimeric flavoenzyme. It shows the properties of the dehydrogenase-oxidase class of flavoproteins, possesses a low kinetic efficiency, and follows a ternary complex (sequential) kinetic mechanism. In contrast to the other known DAAOs, the human enzyme is a stable homodimer even in the apoprotein form and weakly binds the cofactor in the free form.