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[Part 1: Biological Sciences] || A Computer Model Analysis of the Active-Site Coupling Mechanism in the Pyruvate Dehydrogenase Multienzyme Complex of Escherichia coli

โœ Scribed by Marvin L. Hackert, Robert M. Oliver and Lester J. Reed


Book ID
123745073
Publisher
National Academy of Sciences
Year
1983
Tongue
English
Weight
866 KB
Volume
80
Category
Article
ISSN
0027-8424

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Active-site changes in the pyruvate dehy
โœ Chandrasekhar, Krishnamoorthy ;Arjunan, Palaniappa ;Sax, Martin ;Nemeria, Natali ๐Ÿ“‚ Article ๐Ÿ“… 2006 ๐Ÿ› International Union of Crystallography ๐ŸŒ English โš– 587 KB

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