PMID:6365919
| Citation |
Apfel, MA, Ikeda, BH, Speckhard, DC and Frey, PA (1984) Escherichia coli pyruvate dehydrogenase complex. Thiamin pyrophosphate-dependent inactivation by 3-bromopyruvate. J. Biol. Chem. 259:2905-9 |
|---|---|
| Abstract |
Inactivation of the pyruvate dehydrogenase complex by 3-bromopyruvate is thiamin pyrophosphate (TPP)-dependent. Inactivation with 2-14C- or 3-14C-labeled 3-bromopyruvate results in TPP-dependent covalent labeling of more than 60 sites in the complex, all of which are associated with the dihydrolipoyl transacetylase component. Inactivation by 3-bromo[1-14C]pyruvate labels up to 20 sites associated with dihydrolipoyl transacetylase, also with TPP dependence. Systemic chemical degradation of the complex inactivated by 3-bromo[2-14C]pyruvate under conditions that would convert lipoyl groups to S,S,-biscarboxymethyl dihydrolipoic acid produces S,S,-bis[14C]carboxymethyl dihydrolipoic acid. It is concluded that 3-bromopyruvate inactivates this complex by initially undergoing the first two steps of the usual catalytic pathway, TPP-dependent decarboxylation followed by reductive bromoacetylation of lipoyl moieties. The sulfhydryl groups of S-bromoacetyl dihydrolipoyl moieties generated by reductive bromoacetylation are then alkylated by 3-bromopyruvate as well as by bromoacetyl thioester groups associated with the complex. |
| Links | |
| Keywords |
Affinity Labels/pharmacology; Alkylation; Carbon Radioisotopes/diagnostic use; Escherichia coli/enzymology; Kinetics; Pyruvate Dehydrogenase Complex/metabolism; Pyruvates/pharmacology; Thiamine Pyrophosphate/antagonists & inhibitors |
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