Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase multienzyme complexes
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00430a023
Reference53 articles.
1. Elementary steps in the reaction mechanism of the pyruvate dehydrogenase multienzyme complex from Escherichia coli: kinetics of acetylation and deacetylation
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3. Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli.
4. Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from bovine heart.
5. Use of dimethyl suberimidate and novel periodate-cleavable bis(imido esters) to study the quaternary structure of the pyruvate dehydrogenase multienzyme complex of Escherichia coli
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