Crystal structure of the catalase–peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942 in complex with the antitubercular pro‐drug isoniazid-Reference-Cited by-同舟云学术

Crystal structure of the catalase–peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942 in complex with the antitubercular pro‐drug isoniazid

Published:2014-12-03 Issue:1 Volume:589 Page:131-137
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Letters

Author:

Kamachi Saori¹,Hirabayashi Kei²³,Tamoi Masahiro⁴,Shigeoka Shigeru⁴,Tada Toshiji¹,Wada Kei²

Affiliation:

1. Graduate School of Science, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan

2. Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki 889-1692, Japan

3. Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan

4. Faculty of Agriculture, Kinki University, Nakamachi, Nara 631-8505, Japan

Funder

Ministry of Education, Culture, Sports, Science, and Technology

MEXT Grants-in-Aid of Scientific Research

Japan Foundation for Applied Enzymology

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2014.11.037

Reference36 articles.

1. The catalase—peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis

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

3. The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: Adduct affinity and drug resistance

4. Isonicotinic Acid Hydrazide Conversion to Isonicotinyl-NAD by Catalase-peroxidases

5. Reduced Affinity for Isoniazid in the S315T Mutant ofMycobacterium tuberculosis KatG Is a Key Factor in Antibiotic Resistance

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