Literature DB >> 24185282

Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid.

Xiangbo Zhao1, Hans-Petter Hersleth, Janan Zhu, K Kristoffer Andersson, Richard S Magliozzo.   

Abstract

Peroxidatic activation of the anti-tuberculosis pro-drug isoniazid by Mycobacterium tuberculosis catalase-peroxidase (KatG) is regulated by gating residues of a heme access channel. The steric restriction at the bottleneck of this channel is alleviated by replacement of residue Asp137 with Ser, according to crystallographic and kinetic studies.

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Year:  2013        PMID： 24185282      PMCID： PMC3872143          DOI： 10.1039/c3cc47022a

Source DB:  PubMed          Journal:  Chem Commun (Camb)        ISSN： 1359-7345            Impact factor:   6.222


  29 in total

1.  Total conversion of bifunctional catalase-peroxidase (KatG) to monofunctional peroxidase by exchange of a conserved distal side tyrosine.

Authors:  Christa Jakopitsch; Markus Auer; Anabella Ivancich; Florian Rüker; Paul Georg Furtmüller; Christian Obinger
Journal:  J Biol Chem       Date:  2003-03-20       Impact factor: 5.157

Review 2.  Structures of the high-valent metal-ion haem-oxygen intermediates in peroxidases, oxygenases and catalases.

Authors:  Hans-Petter Hersleth; Ulf Ryde; Patrik Rydberg; Carl Henrik Görbitz; K Kristoffer Andersson
Journal:  J Inorg Biochem       Date:  2006-02-28       Impact factor: 4.155

3.  Characterization of the W321F mutant of Mycobacterium tuberculosis catalase-peroxidase KatG.

Authors:  Shengwei Yu; Salem Chouchane; Richard S Magliozzo
Journal:  Protein Sci       Date:  2002-01       Impact factor: 6.725

4.  Reduced affinity for Isoniazid in the S315T mutant of Mycobacterium tuberculosis KatG is a key factor in antibiotic resistance.

Authors:  Shengwei Yu; Stefania Girotto; Chiuhong Lee; Richard S Magliozzo
Journal:  J Biol Chem       Date:  2003-02-13       Impact factor: 5.157

5.  Kinetics of interconversion of ferrous enzymes, compound II and compound III, of wild-type synechocystis catalase-peroxidase and Y249F: proposal for the catalatic mechanism.

Authors:  Christa Jakopitsch; Anuruddhika Wanasinghe; Walter Jantschko; Paul G Furtmüller; Christian Obinger
Journal:  J Biol Chem       Date:  2005-01-06       Impact factor: 5.157

6.  Roles for Arg426 and Trp111 in the modulation of NADH oxidase activity of the catalase-peroxidase KatG from Burkholderia pseudomallei inferred from pH-induced structural changes.

Authors:  Xavier Carpena; Ben Wiseman; Taweewat Deemagarn; Beatriz Herguedas; Anabella Ivancich; Rahul Singh; Peter C Loewen; Ignacio Fita
Journal:  Biochemistry       Date:  2006-04-25       Impact factor: 3.162

7.  A mechanistic study on the oxidation of hydrazides: application to the tuberculosis drug isoniazid.

Authors:  Ruth I J Amos; Brendon S Gourlay; Carl H Schiesser; Jason A Smith; Brian F Yates
Journal:  Chem Commun (Camb)       Date:  2008-02-08       Impact factor: 6.222

8.  Isoniazid activation defects in recombinant Mycobacterium tuberculosis catalase-peroxidase (KatG) mutants evident in InhA inhibitor production.

Authors:  Chih-Jen Wei; Benfang Lei; James M Musser; Shiao-Chun Tu
Journal:  Antimicrob Agents Chemother       Date:  2003-02       Impact factor: 5.191

9.  Two [Fe(IV)=O Trp*] intermediates in M. tuberculosis catalase-peroxidase discriminated by multifrequency (9-285 GHz) EPR spectroscopy: reactivity toward isoniazid.

Authors:  Rahul Singh; Jack Switala; Peter C Loewen; Anabella Ivancich
Journal:  J Am Chem Soc       Date:  2007-12-04       Impact factor: 15.419

10.  The tuberculosis prodrug isoniazid bound to activating peroxidases.

Authors:  Clive Metcalfe; Isabel K Macdonald; Emma J Murphy; Katherine A Brown; Emma Lloyd Raven; Peter C E Moody
Journal:  J Biol Chem       Date:  2007-12-05       Impact factor: 5.157
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  6 in total

1.  Differential Sensitivity of Mycobacteria to Isoniazid Is Related to Differences in KatG-Mediated Enzymatic Activation of the Drug.

Authors:  Tali H Reingewertz; Tom Meyer; Fiona McIntosh; Jaryd Sullivan; Michal Meir; Yung-Fu Chang; Marcel A Behr; Daniel Barkan
Journal:  Antimicrob Agents Chemother       Date:  2020-01-27       Impact factor: 5.191

2.  Mutations in catalase-peroxidase KatG from isoniazid resistant Mycobacterium tuberculosis clinical isolates: insights from molecular dynamics simulations.

Authors:  Arethusa Lobo Pimentel; Regiane Bertin de Lima Scodro; Katiany Rizzieri Caleffi-Ferracioli; Vera Lúcia Dias Siqueira; Paula Aline Zanetti Campanerut-Sá; Luciana Dias Ghiraldi Lopes; Aryadne Larissa de Almeida; Rosilene Fressatti Cardoso; Flavio Augusto Vicente Seixas
Journal:  J Mol Model       Date:  2017-03-16       Impact factor: 1.810

3.  KatG as Counterselection Marker for Nontuberculous Mycobacteria.

Authors:  Aron Gagliardi; Petra Selchow; Sakshi Luthra; Daniel Schäfle; Bettina Schulthess; Peter Sander
Journal:  Antimicrob Agents Chemother       Date:  2020-04-21       Impact factor: 5.191

4.  Modeling the structural origins of drug resistance to isoniazid via key mutations in Mycobacterium tuberculosis catalase-peroxidase, KatG.

Authors:  Matthew W Marney; Robert P Metzger; David Hecht; Faramarz Valafar
Journal:  Tuberculosis (Edinb)       Date:  2017-11-22       Impact factor: 3.131

5.  Deciphering Isoniazid Drug Resistance Mechanisms on Dimeric Mycobacterium tuberculosis KatG via Post-molecular Dynamics Analyses Including Combined Dynamic Residue Network Metrics.

Authors:  Victor Barozi; Thommas Mutemi Musyoka; Olivier Sheik Amamuddy; Özlem Tastan Bishop
Journal:  ACS Omega       Date:  2022-04-07

6.  Using cryo-EM to understand antimycobacterial resistance in the catalase-peroxidase (KatG) from Mycobacterium tuberculosis.

Authors:  Asma Munir; Michael T Wilson; Steven W Hardwick; Dimitri Y Chirgadze; Jonathan A R Worrall; Tom L Blundell; Amanda K Chaplin
Journal:  Structure       Date:  2021-01-13       Impact factor: 5.006
  6 in total

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