Escherichia coli pyruvate dehydrogenase complex. Thiamin pyrophosphate-dependent inactivation by 3-bromopyruvate.
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چکیده
منابع مشابه
Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase.
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 chemica...
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Bromopyruvate inactivates the pyruvate dehydrogenase complex of Escherichia coli in a thiamine pyrophosphate (TPP)-dependent process. The catalytic activities of the individual enzyme components within the complex are not destroyed by bromopyruvate under similar conditions, but the activities of the pyruvate dehydrogenase and dihydrolipoyl dehydrogenase components are reduced in thiamine pyroph...
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ATP inactivated plant pyruvate dehydrogenase complex (PDC) from broccoli (Brassica oleracea) mitochondria. ATP inactivation of the complex was time-dependent and proportional to the ATP concentration. Time-dependent incorporation of (32)P from [gamma(32)P]ATP into trichloroacetic acid-precipitable protein corresponded to the inactivation of the PDC. It is concluded that plant PDC is phosphoryla...
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The binding of pyruvate dehydrogenase and dihydrolipoyl dehydrogenase (flavoprotein) to dihydrolipoyl transacetylase, the core enzyme of the E. coli pyruvate dehydrogenase complex [EC 1.2.4.1:pyruvate:lipoate oxidoreductase (decaryboxylating and acceptor-acetylating)], has been studied using sedimentation equilibrium analysis and radioactive enzymes in conjunction with gel filtration chromatogr...
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The investigation of the substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli allows a description of the binding region of pyruvate. Substrate analogs with electronegative substitutions in the methyl group show a strong competitive inhibition of the overall reaction of the pyruvate dehydrogenase complex. The most efficient inhibitor is fluoropyruvate which has a mo...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1984
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)43234-0