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Science 12 February 1993:
Vol. 259. no. 5097, pp. 965 - 967
DOI: 10.1126/science.8438155
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Articles

Science, Vol 259, Issue 5097, 965-967
Copyright © 1993 by American Association for the Advancement of Science

articles

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

YA Muller and GE Schulz

Institut fur Organische Chemie und Biochemie, Albert-Ludwigs-Universitat, Freiburg, Germany.

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.


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