PMID: 9523710Apr 2, 1998Paper

Kinetics and specificity of reductive acylation of wild-type and mutated lipoyl domains of 2-oxo-acid dehydrogenase complexes from Azotobacter vinelandii

European Journal of Biochemistry
A BergA de Kok

Abstract

The kinetics and specificity of reductive acylation of lipoyl domains derived from Azotobacter vinelandii 2-oxo-acid dehydrogenase complexes, catalysed by A. vinelandii and Escherichia coli complexes, have been investigated. With the wild-type pyruvate dehydrogenase complex from A. vinelandii the rate of reductive acetylation and deacetylation was studied by rapid mixing methods. The rate of reductive acetylation, 126 s(-1), corresponds well with the turnover rate derived from steady-state measurements. Deacetylation was rapid and specific for coenzyme A. No deacetylation was observed with reduced or oxidised lipoamide or with dithiothreitol. The rate of reductive acetylation of complex-bound lipoyl domains by pyruvate dehydrogenase (E1p) is at least 60 times higher than of free lipoyl domains under comparable conditions. This gain in catalytic rate indicates a large diffusion limitation of lipoyl domains when attached via the flexible linker segments to the complex, and illustrates the efficiency of substrate channeling in the multienzyme complex. The 2-oxo-acid dehydrogenases exhibit specificity for lipoyl domains in the reductive acylation reaction. The A. vinelandii lipoyl domain derived from the pyruvate dehydrogenase comp...Continue Reading

Citations

Jun 8, 2001·Annual Review of Biochemistry·X HuangF M Raushel
Apr 15, 2016·Microbiology and Molecular Biology Reviews : MMBR·John E Cronan
Sep 3, 1999·The Journal of Biological Chemistry·V GueguenJ Bourguignon
Oct 16, 1999·European Journal of Biochemistry·A F HengeveldA de Kok
Jul 10, 1998·Biochimica Et Biophysica Acta·A de KokA H Westphal
May 23, 2001·Archives of Biochemistry and Biophysics·S LiuT E Roche

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