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Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase.

Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS
J Biol Chem 278 21240-6 (2003)
Cited: 86 times
EuropePMC logo PMID: 12651851

Abstract

The derivative of vitamin B1, thiamin pyrophosphate, is a cofactor of enzymes performing catalysis in pathways of energy production. In alpha2beta2-heterotetrameric human pyruvate dehydrogenase, this cofactor is used to cleave the Calpha-C(=O) bond of pyruvate followed by reductive acetyl transfer to lipoyl-dihydrolipoamide acetyltransferase. The dynamic nonequivalence of two, otherwise chemically equivalent, catalytic sites has not yet been understood. To understand the mechanism of action of this enzyme, we determined the crystal structure of the holo-form of human pyruvate dehydrogenase at 1.95-A resolution. We propose a model for the flip-flop action of this enzyme through a concerted approximately 2-A shuttle-like motion of its heterodimers. Similarity of thiamin pyrophosphate binding in human pyruvate dehydrogenase with functionally related enzymes suggests that this newly defined shuttle-like motion of domains is common to the family of thiamin pyrophosphate-dependent enzymes.

Reviews - 1ni4 mentioned but not cited (1)

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Articles - 1ni4 mentioned but not cited (19)

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  1. Molecular cloning and characterization of human pyruvate dehydrogenase beta subunit gene.. Koike K, Urata Y, Koike M Proc Natl Acad Sci U S A 87 5594-7 (1990)

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