Further evidence in favour of a carbanion mechanism for glycolate oxidase.

ABSTRACT: The flavoenzyme glycolate oxidase oxidizes glycolic acid to glyoxylate and the latter, more slowly, to oxalate. It is a member of an FMN-dependent enzyme family that oxidizes l-2-hydroxy acids to keto acids. There has been a controversy concerning the chemical mechanism of substrate oxidation by these enzymes. Do they proceed by hydride transfer, as observed for NAD-dependent enzymes, or by initial formation of a carbanion that transfers the electrons to the flavin? The present work describes a comparison of the reactivity of glycolate, lactate and trifluorolactate with recombinant human glycolate oxidase, by means of rapid-kinetics experiments in anaerobiosis. We show that trifluorolactate is a substrate for glycolate oxidase, whereas it is known as an inhibitor for NAD-dependent enzymes,

SUBMITTER: Pasquier H 

PROVIDER: S-EPMC10153336 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature