Inhibitor Binding Studies on Enoyl Reductase Reveal Conformational Changes Related to Substrate Recognition-Reference-Cited by-同舟云学术

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Inhibitor Binding Studies on Enoyl Reductase Reveal Conformational Changes Related to Substrate Recognition

Published:1999-10 Issue:43 Volume:274 Page:30811-30817
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Roujeinikova Anna,Sedelnikova Svetlana,de Boer Gert-Jan,Stuitje Antoine R.,Slabas Antoni R.,Rafferty John B.,Rice David W.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference26 articles.

1. Fatty Acid Metabolism

2. Enzymic Characterization of the Target for Isoniazid in Mycobacterium tuberculosis

3. Protein EnvM is the NADH-dependent enoyl-ACP reductase (FabI) of Escherichia coli.

4. The use of a hybrid genetic system to study the functional relationship between prokaryotic and plant multi-enzyme fatty acid synthetase complexes

5. Molecular basis of triclosan activity

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2. PROTECTIVE ENVIRONMENTS FOR ANIMAL SPERM: EVOLUTION OF METHODS AND TOPICAL ASPECTS (REVIEW ARTICLE);The Scientific and Technical Bulletin of the Institute of Animal Science NAAS of Ukraine;2023

3. Boron-Containing heterocycles as promising pharmacological agents;Bioorganic & Medicinal Chemistry;2022-06

4. Type II fatty acid and polyketide synthases: deciphering protein–protein and protein–substrate interactions;Natural Product Reports;2018

5. Discovery of Mycobacterium tuberculosis InhA Inhibitors by Binding Sites Comparison and Ligands Prediction;Journal of Medicinal Chemistry;2016-12-12

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