Stereoisomers of tetrahydrothiamin pyrophosphate, potent inhibitors of the pyruvate dehydrogenase multienzyme complex from Escherichia coli
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00270a022
Reference30 articles.
1. On the Mechanism of Thiamine Action. IV.1 Evidence from Studies on Model Systems
2. Binding of thiamin thiazolone pyrophosphate to mammalian pyruvate dehydrogenase and its effects on kinase and phosphatase activities
3. The reduction of thiazolium salts with sodium borohydride. Part II. The mechanism and stereochemistry of reduction
4. 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
5. Mechanisms of thiamine-catalyzed reactions. Kinetic analysis of the decarboxylation of pyruvate by 3,4-dimethylthiazolium ion in water and ethanol
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