Literature summary for 1.2.1.104 extracted from

Stevenson, K.; Hale, G.; Perham, R.
Inhibition of pyruvate dehydrogenase multienzyme complex from Escherichia coli with mono- and bifunctional arsenoxides (1978), Biochemistry, 17, 2189-2192 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
4-aminophenyl arsenoxide	0.1 mM, 92% loss of activity in presence of pyruvate and CoA. Controls lacking pyruvate and/or coenzyme A, but containing H2NPhAsO, retain nearly all their pyruvate dehydrogenase complex activity. The arsenoxide forms a stable cyclic dithiolarsinite with reduced lipoic acid on E2 which is generated by pyruvate and coenzyme A according. Pyruvate dehydrogenase complex activity can be recovered to 78% within 2 min following the addition of 2,3-dithiopropanol	Escherichia coli
bromoacetylaniline arsenoxide	BrCH2CONHPhAsO, 0.1 mM, 100% loss of activity in presence of pyruvate and CoA. The initial reaction of the bifunctional reagent occurs on E2 via the R-AsO moiety and results in the rapid loss in pyruvate dehydrogenase complex activity. Addition of 2,3-dithiopropanol fails to regenerate the complex activity and E3 activity	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P06959	P06959 i.e. dihydrolipoyllysine-residue acetyltransferase component	-

Synonyms

Synonyms	Comment	Organism
AceF	-	Escherichia coli

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Release 2023.1 (January 2023)