Abstract
Sodium dehydroacetate has been found to inhibit one of flavin enzymes, D-amino acid oxidase. This inhibition was analyzed by enzyme reaction kinetics using the enzyme purified from hog kidney. Sodium dehydroacetate was found to inhibit D-amino acid oxidase by two inhibitive factors, (1) the one factor based on direct combination of sodium dehydroacetate and coenzyme flavin adenine dinucleotide (FAD), and (2) the factor based on competitive reaction between sodium dehydroacetate and FAD, in saturated system of the substrate. The dissociationconstant of FAD-sodium dehydroacetate complex was measured by the enzyme reaction kinetic method as Kif=2.7×10-2M/liter, and this value agreed approximately with Kif. FAD=3.85×10-2M/liter measured earlier by the physicochemical method (fluorescence method) for the same complex. The dissociation constant of the apoenzymesodium dehydroacetate complex formed by competition between sodium dehydroacetate and FAD was measured as Kip=5.9×10-2M/liter. The flavin-sodium dehydroacetate interaction, previously proved physicochemically, was also proved by enzyme reaction kinetics through inhibition of sodium dehydroacetate against D-amino acid oxidase.
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