Evidence from Raman Spectroscopy That InhA, the Mycobacterial Enoyl Reductase, Modulates the Conformation of the NADH Cofactor to Promote Catalysis
Author:
Affiliation:
1. Contribution from the Department of Chemistry, Stony Brook University, Stony Brook, New York 11794-3400
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja068219m
Reference36 articles.
1. Mutation of tyrosine-194 and lysine-198 in the catalytic site of pig 3α/β,20β-hydroxysteroid dehydrogenase
2. Crystal Structure of the Mycobacterium tuberculosis Enoyl-ACP Reductase, InhA, in Complex with NAD+ and a C16 Fatty Acyl Substrate
3. inhA , a Gene Encoding a Target for Isoniazid and Ethionamide in Mycobacterium tuberculosis
4. Crystal Structure and Function of the Isoniazid Target of Mycobacterium tuberculosis
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1. Bacterial Enoyl-Reductases: The Ever-Growing List of Fabs, Their Mechanisms and Inhibition;Frontiers in Microbiology;2022-06-16
2. InhA, the enoyl-thioester reductase from Mycobacterium tuberculosis forms a covalent adduct during catalysis;Journal of Biological Chemistry;2018-11
3. An overview on crystal structures of InhA protein: Apo-form, in complex with its natural ligands and inhibitors;European Journal of Medicinal Chemistry;2018-02
4. An Ordered Water Channel in Staphylococcus aureus FabI: Unraveling the Mechanism of Substrate Recognition and Reduction;Biochemistry;2015-03-03
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