Direct Kinetic Evidence for Half-Of-The-Sites Reactivity in the E1 Component of the Human Pyruvate Dehydrogenase Multienzyme Complex through Alternating Sites Cofactor Activation†

Biochemistry ◽  
2006 ◽  
Vol 45 (42) ◽  
pp. 12775-12785 ◽  
Author(s):  
Franziska Seifert ◽  
Ralph Golbik ◽  
Johanna Brauer ◽  
Hauke Lilie ◽  
Kathrin Schröder-Tittmann ◽  
...  
Keyword(s):  
Pyruvate Dehydrogenase ◽  
Multienzyme Complex

The Pyruvate Dehydrogenase Multienzyme Complex

2003 ◽  
Author(s):  
Richard Perham ◽  
Jacqueline Milne ◽  
Sriram Subramaniam
Keyword(s):  
Pyruvate Dehydrogenase ◽  
Multienzyme Complex

Role of pyruvate transporter in the regulation of pyruvate dehydrogenase multienzyme complex in perfused rat liver

Biochemistry ◽  
1982 ◽  
Vol 21 (2) ◽  
pp. 346-353 ◽  
Author(s):  
Franz Maximilian Zwiebel ◽  
Ursula Schwabe ◽  
Merle S. Olson ◽  
Roland Scholz
Keyword(s):  
Rat Liver ◽  
Pyruvate Dehydrogenase ◽  
Multienzyme Complex ◽  
Perfused Rat Liver

scholarly journals Evidence for two lipoic acid residues per lipoate acetyltransferase chain in the pyruvate dehydrogenase multienzyme complex of Escherichia coli

1976 ◽  
Vol 159 (3) ◽  
pp. 677-682 ◽  
Author(s):  
M J Danson ◽  
R N Perham
Keyword(s):  
Escherichia Coli ◽  
Lipoic Acid ◽  
Pyruvate Dehydrogenase ◽  
Acid Content ◽  
Polypeptide Chain ◽  
Multienzyme Complex ◽  
Covalently Bound

The reaction of two maleimides, N-ethylmaleimide and bis-(N-maleimidomethyl) ether, with the pyruvate dehydrogenase multienzyme complex of Escherichia coli in the presence of the substrate, pyruvate, was examined. In both cases, the reaction was demonstrated to be almost exclusively with the lipoate acetyltransferase component, and evidence is presented to show that the most likely sites of reaction are the lipoic acid residues covalently bound to this component. With both reagents the stoicheiometry of the reaction was measured: 2 mol of reagent reacted with each polypeptide chain of lipoate acetyltransferase, implying that each chain bears two functionally active lipolic acid residues. This observation can be reconciled with previous determinations of the lipoic acid content of the complex by allowing for the variability of the subunit polypeptide-chain ratio that can be demonstrated for this multimeric enzyme.

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