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Inhibition of pyruvate dehydrogenase multienzyme complex from Escherichia coli with a radiolabeled bifunctional arsenoxide: evidence for essential histidine residue at the active site of lipoamide dehydrogenase

โœ Scribed by Adamson, S. Robert; Robinson, James A.; Stevenson, Kenneth J.


Book ID
127053103
Publisher
American Chemical Society
Year
1984
Tongue
English
Weight
820 KB
Volume
23
Category
Article
ISSN
0006-2960

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The first enzymatic component, E1 (EC 1.2.4.1), of the pyruvate dehydrogenase multienzyme complex (PDHc) utilizes thiamine diphosphate (ThDP) and Mg(2+) as cofactors. The structure of a branched-chain-specific E1 apoenzyme from the heterotetrameric alpha(2)beta(2) E1 family was recently reported and