Mycobacterium tuberculosis KatG(S315T) Catalase−Peroxidase Retains All Active Site Properties for Proper Catalytic Function-Reference-Cited by-同舟云学术

Mycobacterium tuberculosis KatG(S315T) Catalase−Peroxidase Retains All Active Site Properties for Proper Catalytic Function

Published:2004-12-04 Issue:1 Volume:44 Page:243-252
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kapetanaki Sofia M.¹,Chouchane Salem¹,Yu Shengwei¹,Zhao Xiangbo¹,Magliozzo Richard S.¹,Schelvis Johannes P. M.¹

Affiliation:

1. Department of Chemistry, New York University, Room 1001, 31 Washington Place, New York, New York 10003, and Department of Chemistry, Brooklyn College and the Graduate Center of the City University of New York, 2900 Bedford Avenue, Brooklyn, New York 11210-2889

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi048097f

Reference83 articles.

1. Mechanistic Studies of the Oxidation of Isoniazid by the Catalase Peroxidase from Mycobacterium tuberculosis

2. Binding of Catalase-Peroxidase-Activated Isoniazid to Wild-Type and Mutant Mycobacterium tuberculosis Enoyl-ACP Reductases

3. Kinetics of Inactivation of WT and C243S Mutant of Mycobacterium tuberculosis Enoyl Reductase by Activated Isoniazid

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