Complex formation between reduced D-amino acid oxidase and pyridine carboxylates.
Picolinate binds to a reduced form of D-amino acid oxidase, and the complex formed has a broad absorption band around 600 nm as in the case of the purple intermediate of the enzyme with a substrate. The dissociation constant at 25 degrees C was 35 microns at pH 7.0. The pH dependence (pH 8.3-pH 6.4) of the dissociation constant indicates that one proton is associated with the complex formation, and picolinate protonated at the N atom binds to the reduced enzyme. Resonance Raman spectra of the complex support that picolinate in the complex is a cationic form protonated at the N atom. Nicotinate also binds to the reduced enzyme, but isonicotinate does not.
Nishina
Y
Y
Tojo
H
H
Shiga
K
K
D000818:Animals; D003605:D-Amino-Acid Oxidase; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D009243:NAD; D009525:Niacin; D010084:Oxidation-Reduction; D010848:Picolinic Acids; D011725:Pyridines; D013053:Spectrophotometry; D013059:Spectrum Analysis, Raman; D013329:Structure-Activity Relationship; D013552:Swine
D008024:Ligands; D010848:Picolinic Acids; D011725:Pyridines; D009243:NAD; D009525:Niacin; D003605:D-Amino-Acid Oxidase; C023666:pyridine; C030614:picolinic acid