Literature DB >> 10080924

Mycobacterium tuberculosis KatG is a peroxynitritase.

N L Wengenack1, M P Jensen, F Rusnak, M K Stern.   

Abstract

Mycobacterium tuberculosis resides within the highly oxidative environment of the human macrophage and previous reports have indicated that these mycobacteria are susceptible to reactive nitrogen intermediates including peroxynitrite. This work provides evidence that the Mycobacterium tuberculosis hemoprotein KatG acts as an efficient peroxynitritase exhibiting a kapp of 1.4 x 10(5) M-1s-1 for peroxynitrite decomposition at pH 7.4 and 37 degrees C. The ability of KatG to act as a peroxynitritase adds to its growing list of enzymatic activities and may in part explain the ability of Mycobacterium tuberculosis to persist in macrophages. Copyright 1999 Academic Press.

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Year:  1999        PMID: 10080924     DOI: 10.1006/bbrc.1999.0358

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  20 in total

1.  Exploring the structure and function of the mycobacterial KatG protein using trans-dominant mutants.

Authors:  Joseph A DeVito; Sheldon Morris
Journal:  Antimicrob Agents Chemother       Date:  2003-01       Impact factor: 5.191

2.  Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst.

Authors:  D L Piddington; F C Fang; T Laessig; A M Cooper; I M Orme; N A Buchmeier
Journal:  Infect Immun       Date:  2001-08       Impact factor: 3.441

3.  The role of catalase in gonococcal resistance to peroxynitrite.

Authors:  Stephen A Spence; Virginia L Clark; Vincent M Isabella
Journal:  Microbiology       Date:  2011-11-24       Impact factor: 2.777

4.  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

5.  Peroxynitrite toxicity in Escherichia coli K12 elicits expression of oxidative stress responses and protein nitration and nitrosylation.

Authors:  Samantha McLean; Lesley A H Bowman; Guido Sanguinetti; Robert C Read; Robert K Poole
Journal:  J Biol Chem       Date:  2010-04-28       Impact factor: 5.157

6.  Mapping of Mycobacterium tuberculosis katG promoters and their differential expression in infected macrophages.

Authors:  S Master; T C Zahrt; J Song; V Deretic
Journal:  J Bacteriol       Date:  2001-07       Impact factor: 3.490

7.  Isoniazid-resistance conferring mutations in Mycobacterium tuberculosis KatG: catalase, peroxidase, and INH-NADH adduct formation activities.

Authors:  Christine E Cade; Adrienne C Dlouhy; Katalin F Medzihradszky; Saida Patricia Salas-Castillo; Reza A Ghiladi
Journal:  Protein Sci       Date:  2010-03       Impact factor: 6.725

8.  Requirements for nitric oxide generation from isoniazid activation in vitro and inhibition of mycobacterial respiration in vivo.

Authors:  Graham S Timmins; Sharon Master; Frank Rusnak; Vojo Deretic
Journal:  J Bacteriol       Date:  2004-08       Impact factor: 3.490

9.  Nitric oxide generated from isoniazid activation by KatG: source of nitric oxide and activity against Mycobacterium tuberculosis.

Authors:  Graham S Timmins; Sharon Master; Frank Rusnak; Vojo Deretic
Journal:  Antimicrob Agents Chemother       Date:  2004-08       Impact factor: 5.191

10.  Transcriptional characterization of the antioxidant response of Mycobacterium tuberculosis in vivo and during adaptation to hypoxia in vitro.

Authors:  Lanbo Shi; Charles D Sohaskey; Robert J North; Maria L Gennaro
Journal:  Tuberculosis (Edinb)       Date:  2007-10-24       Impact factor: 3.131

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