Evaluating the Impact of the Tyr158 pKa on the Mechanism and Inhibition of InhA, the Enoyl-ACP Reductase from Mycobacterium tuberculosis-Reference-Cited by-同舟云学术

Evaluating the Impact of the Tyr158 pK_a on the Mechanism and Inhibition of InhA, the Enoyl-ACP Reductase from Mycobacterium tuberculosis

Published:2023-06-04 Issue:12 Volume:62 Page:1943-1952
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Davoodi Shabnam¹²,Daryaee Fereidoon¹²,Iuliano James N.¹²^ORCID,Tolentino Collado Jinnette¹²,He YongLe¹²,Pollard Alyssa C.¹²,Gil Agnieszka A.²^ORCID,Aramini James M.³,Tonge Peter J.¹²⁴^ORCID

Affiliation:

1. Center for Advanced Study of Drug Action, Stony Brook University, John S. Toll Drive, Stony Brook, New York 11794-3400, United States

2. Department of Chemistry, Stony Brook University, John S. Toll Drive, Stony Brook, New York 11794-3400, United States

3. Structural Biology Initiative, CUNY Advanced Science Research Center, New York, New York 10031, United States

4. Department of Radiology, Stony Brook University, John S. Toll Drive, Stony Brook, New York 11794-3400, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.2c00606

Reference44 articles.

1. The WHO 2014 Global tuberculosis report—further to go

2. Roles of Tyrosine 158 and Lysine 165 in the Catalytic Mechanism of InhA, the Enoyl-ACP Reductase from Mycobacterium tuberculosis

3. Modification of the NADH of the Isoniazid Target (InhA) from Mycobacterium tuberculosis

4. An overview on crystal structures of InhA protein: Apo-form, in complex with its natural ligands and inhibitors

5. Genetic Mutations Associated with Isoniazid Resistance in Mycobacterium tuberculosis: A Systematic Review

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