Identification of a Mycothiol-Dependent Nitroreductase from Mycobacterium tuberculosis | Zendy

Aegri | Zendy; Prisca Elis Javidnia | Zendy; Ran Mu | Zendy; Xiaojie Zhang | Zendy; Jérémie Vendôme | Zendy; Ben Gold | Zendy; Julia Roberts | Zendy; Dipti Barman | Zendy; Thomas R. Ioerger | Zendy; James C. Sacchettini | Zendy; Xiuju Jiang | Zendy; Kristin Burns-Huang | Zendy; Thulasi Warrier | Zendy; Yan Ling | Zendy; J. David Warren | Zendy; Deena A. Oren | Zendy; Thijs Beuming | Zendy; Hongyao Wang | Zendy; Jie Wu | Zendy; Haitao Li | Zendy; Kyu Y. Rhee | Zendy; Carl Nathan | Zendy; Gang Liu | Zendy; Selin Somersan-Karakaya | Zendy

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Identification of a Mycothiol-Dependent Nitroreductase from Mycobacterium tuberculosis

Author(s) -

Aegri,

Prisca Elis Javidnia,

Ran Mu,

Xiaojie Zhang,

Jérémie Vendôme,

Ben Gold,

Julia Roberts,

Dipti Barman,

Thomas R. Ioerger,

James C. Sacchettini,

Xiuju Jiang,

Kristin Burns-Huang,

Thulasi Warrier,

Yan Ling,

J. David Warren,

Deena A. Oren,

Thijs Beuming,

Hongyao Wang,

Jie Wu,

Haitao Li,

Kyu Y. Rhee,

Carl Nathan,

Gang Liu,

Selin Somersan-Karakaya

Publication year - 2018

Publication title -

acs infectious diseases

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.324

H-Index - 39

ISSN - 2373-8227

DOI - 10.1021/acsinfecdis.7b00111

Subject(s) - nitroreductase , mycobacterium tuberculosis , microbiology and biotechnology , cofactor , biology , menadione , mycobacterium , tuberculosis , enzyme , biochemistry , genetics , bacteria , medicine , pathology

The success of Mycobacterium tuberculosis (Mtb) as a pathogen depends on the redundant and complex mechanisms it has evolved for resisting nitrosative and oxidative stresses inflicted by host immunity. Improving our understanding of these defense pathways can reveal vulnerable points in Mtb pathogenesis. In this study, we combined genetic, structural, computational, biochemical, and biophysical approaches to identify a novel enzyme class represented by Rv2466c. We show that Rv2466c is a mycothiol-dependent nitroreductase of Mtb and can reduce the nitro group of a novel mycobactericidal compound using mycothiol as a cofactor. In addition to its function as a nitroreductase, Rv2466c confers partial protection to menadione stress.

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