Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase.

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Muller YA, Schulz GE

Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase.

Science. 1993 Feb 12;259(5097):965-7. doi: 10.1126/science.8438155.

PubMed ID
8438155 [ View in PubMed
]
Abstract

Pyruvate oxidase from Lactobacillus plantarum is a tetrameric enzyme that decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. Structure determination at 2.1 angstroms showed that the cofactors thiamine pyrophosphate (TPP) and flavin adenine dinucleotide (FAD) are bound at the carboxyl termini of six-stranded parallel beta sheets. The pyrophosphate moiety of TPP is bound to a metal ion and to a beta alpha alpha beta unit corresponding to an established sequence fingerprint. The spatial arrangement of TPP and FAD suggests that the oxidation of the oxyethyl intermediate does not occur by hydride displacement but rather by a two-step transfer of two electrons.

DrugBank Data that Cites this Article

Drug Enzymes
DrugEnzymeKindOrganismPharmacological ActionActions
CocarboxylasePyruvate oxidaseProteinLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Unknown
Not AvailableDetails
Polypeptides
NameUniProt ID
Pyruvate oxidaseP37063Details