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Characterization of human d ‐amino acid oxidase
Author(s) -
Molla Gianluca,
Sacchi Silvia,
Bernasconi Mariagrazia,
Pilone Mirella S.,
Fukui Kiyoshi,
Pollegioni Loredano
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.045
Subject(s) - d amino acid oxidase , biochemistry , chemistry , allosteric regulation , ternary complex , oxidase test , enzyme , cofactor , serine , glutamate dehydrogenase , recombinant dna , activator (genetics) , stereochemistry , glutamate receptor , receptor , gene
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.