Characterization of the inhibition of Escherichia coli pyruvate dehydrogenase complex by pyruvate.
The E. coli pyruvate dehydrogenase complex was inhibited by pyruvate in absence of its cofactor, NAD+. The inhibition was found to increase with pH and phosphate concentration of the buffer and decrease with its ionic strength. The inhibition profile was different with MOPS buffer. No radioactivity was found in the enzyme, when the latter was incubated with 2-14C-pyruvate. The results suggest that covalent adduct formation is not necessary for the observed inhibition.
Datta
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University of Wisconsin Biotechnology Center, Madison 53705.
D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009994:Osmolar Concentration; D010710:Phosphates / Q000494:pharmacology; D011485:Protein Binding; D011768:Pyruvate Dehydrogenase Complex / Q000037:antagonists & inhibitors*; D011773:Pyruvates / Q000378:metabolism / Q000494:pharmacology*; D019289:Pyruvic Acid
D010710:Phosphates; D011768:Pyruvate Dehydrogenase Complex; D011773:Pyruvates; D019289:Pyruvic Acid