Impact of Distal Side Water and Residue 315 on Ligand Binding to Ferric Mycobacterium tuberculosis Catalase−Peroxidase (KatG)-Reference-Cited by-同舟云学术

Impact of Distal Side Water and Residue 315 on Ligand Binding to Ferric Mycobacterium tuberculosis Catalase−Peroxidase (KatG)

Published:2008-10-29 Issue:47 Volume:47 Page:12583-12592
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ranguelova Kalina¹,Suarez Javier¹,Metlitsky Leonid¹,Yu Shengwei¹,Brejt Shelly Zev¹,Brejt Sidney Zelig¹,Zhao Lin¹,Schelvis Johannes P. M.¹,Magliozzo Richard S.¹

Affiliation:

1. Department of Chemistry, Brooklyn College, 2900 Bedford Avenue, Brooklyn, New York 11210, Department of Biochemistry, The Graduate Center of the City University of New York, 365 Fifth Avenue, New York, New York 10016, and Department of Chemistry, New York University, 31 Washington Place, New York, New York 10003

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi801511u

Reference44 articles.

1. Site-directed mutagenesis of the katG gene of Mycobacterium tuberculosis : effects on catalase-peroxidase activities and isoniazid resistance

2. Molecular Population Genetic Analysis of Emerged Bacterial Pathogens: Selected Insights

3. katG mutations in isoniazid-resistant Mycobacterium tuberculosis isolates recovered from Finnish patients

4. Crystal Structure of Mycobacterium tuberculosis Catalase-Peroxidase

5. Hydrogen Peroxide-Mediated Isoniazid Activation Catalyzed by Mycobacterium tuberculosis Catalase−Peroxidase (KatG) and Its S315T Mutant,

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