Structural Determinants of Enzyme Binding Affinity: The E1 Component of Pyruvate Dehydrogenase from Escherichia coli in Complex with the Inhibitor Thiamin Thiazolone Diphosphate,-Reference-Cited by-同舟云学术

Structural Determinants of Enzyme Binding Affinity: The E1 Component of Pyruvate Dehydrogenase from Escherichia coli in Complex with the Inhibitor Thiamin Thiazolone Diphosphate,

Published:2004-02-12 Issue:9 Volume:43 Page:2405-2411
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Arjunan Palaniappa¹,Chandrasekhar Krishnamoorthy¹,Sax Martin¹,Brunskill Andrew¹,Nemeria Natalia¹,Jordan Frank¹,Furey William¹

Affiliation:

1. Biocrystallography Laboratory, Veterans Affairs Medical Center, P.O. Box 12055, University Drive C, Pittsburgh, Pennsylvania 15240, Department of Pharmacology, University of Pittsburgh School of Medicine, 1340 BSTWR, Pittsburgh, Pennsylvania 15261, and Department of Chemistry, Rutgers University, Newark, New Jersey 07102

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi030200y

Reference25 articles.

1. Transition state analogs for thiamin pyrophosphate-dependent enzymes.

2. Inhibition of the Escherichia coli Pyruvate Dehydrogenase Complex E1 Subunit and Its Tyrosine 177 Variants by Thiamin 2-Thiazolone and Thiamin 2-Thiothiazolone Diphosphates

3. Studies of the thiamin pyrophosphate binding site of Escherichia coli pyruvate oxidase. Evidence for an essential tryptophan residue.

4. Interaction of thiamin diphosphate and thiamin thiazolone diphosphate with wheat germ pyruvate decarboxylase.

5. The catalytic mechanism of transketolase. Thiamin pyrophosphate-derived transition states for transketolase and pyruvate dehydrogenase are not identical.

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