PMID: 2492417Feb 1, 1989Paper

2-ketoacid dehydrogenase complexes of Escherichia coli: stereospecificities of the three components for (R)-lipoate

Archives of Biochemistry and Biophysics
Y S Yang, P A Frey

Abstract

Stereospecificities of component enzymes in the pyruvate dehydrogenase complex and 2-ketoglutarate dehydrogenase complex from Escherichia coli for lipoate and dihydrolipoate are determined. Assays of the component enzymes using R,S-, R-, or S-lipoate or the enantiomers of dihydrolipoate show that only the R-enantiomers are substrates for these enzymes. Nonenzymatic reactions involving acetyl group transfer and coupled electron and acetyl group transfer between enantiomeric molecules of lipoate or/and dihydrolipoate proceed at significant rates. Coupled acetyl group and electron transfer from enzyme-bound acetyldihydrolipoyl moieties to free lipoate is also observed. The S-enantiomers are neither substrates nor inhibitors; however, products of S-enantiomers are slowly generated in enzymatic reactions owing to nonenzymatic reactions between enzyme-bound acetyldihydrolipoyl-groups and free S-lipoate or S-dihydrolipoate.

References

Oct 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·J H Collins, L J Reed
Feb 3, 1975·Biochemical and Biophysical Research Communications·D C Speckhard, P A Frey
Jun 1, 1959·Archives of Biochemistry and Biophysics·J M SIEGELR M BOCK

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Citations

Sep 25, 2015·International Journal of Molecular Sciences·Ryota UchidaTakashi Hirota
Feb 9, 1996·Biochemical Pharmacology·G P BiewengaA Bast
Sep 1, 1992·Proteins·J E JentoftM S Patel
Jul 10, 2019·Oxidative Medicine and Cellular Longevity·Víctor Manuel Mendoza-NúñezVicente Jesús Hernández-Abad
Apr 15, 1991·Biochemical and Biophysical Research Communications·A Datta

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