Results 111 to 120 of about 8,860 (214)

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

, 2016
Inhibition of the enzyme Mycobacterium tuberculosis InhA (enoyl-acyl carrier protein reductase) due to formation of an isonicotinoyl-NAD adduct (IN-NAD) from isoniazid (INH) and nicotinamide adenine dinucleotide cofactor is considered central to the mode
Richard S. Magliozzo (204160), Xiangbo Zhao (2289805), Hong Yu (6528), Feng Wang (44414), Shengwei Yu (2289808), James C. Sacchettini (37661)   +5 more
core   +1 more source

Prevalence of katG and inhA mutations associated with isoniazid resistance in Mycobacterium tuberculosis clinical isolates in Cameroon

BMC Microbiology
Background The acquisition of isoniazid (INH) resistance is alarming, considering its importance as a key drug that forms the core of multidrug treatment regimens for tuberculosis (TB). Genetic mutations in the katG and inhA promoter regions play crucial
Vanessa Ninkeh Nono, Edouard Akono Nantia, Awelani Mutshembele, Sorelle Nguimfack Teagho, Yannick Willy Kamdem Simo, Brenda Shile Takong, Yvonne Josiane Djieugoue, Yannick Patrick Assolo, Suzanne Magloire Ongboulal, Stanley Nkemnji Awungafac, Sara Eyangoh, Eric Mensah, Ndivhuho Agnes Makhado, Valerie Flore Donkeng Donfack   +13 more
doaj   +1 more source

KatG and KatB localization and their oxyR growth promoting activity.

, 2012
A–D. V. cholerae containing either PBAD-katG-flag (A, C) or PBAD-katB-flag (B, D) were grown on LB agar plates containing 0.1% arabinose. Western-blot analysis to detect FLAG-tagged KatG and KatB as well as a cytoplasmic protein control HapR in the cell ...
Shusu Chen (107240), Francesca P. Rothenbacher (107246), Juan Zhang (48597), Zengtao Zhong (107259), Hui Wang (30400), Jun Zhu (84054), Tiantian Jiang (107252), Biao Kan (107255)   +7 more
core   +1 more source

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

, 2005
Mycobacterium tuberculosis (Mtb) KatG is a catalase-peroxidase that is thought to activate the antituberculosis drug isoniazid (INH). The local environment of Mtb KatG and its most prevalent INH-resistant mutant, KatG(S315T), is investigated with the ...
Magliozzo, Richard S., Yu, Shengwei, Schelvis, Johannes, Zhao, Xiangbo, Kapetanaki, Sofia M., Chouchane, Salem   +5 more
core   +1 more source

The Susceptibility of katG Ser315Thr Mycobacterium tuberculosis mutant Against Anti Tuberculosis Drugs

Indonesian Journal of Biotechnology, 2016
Mycobacterium tuberculosis resistant strains is a matter of great concern for TB control Program since nocure for some multi drug resistance TB (MDR-TB) cases.
Ning Rintiswati, Praseno P
doaj  

Effect of pyrogallol on the expression of KatG and RtxA1 proteins in Vibrio vulnificus.

, 2016
(A) V. vulnificus wt or katG− mutant strains were cultured in HI broth with pyrogallol (50 μg/mL) or catalase (10 μg/mL) in a 37°C shaking incubator for 6 h.
Young Ran Kim (590460), Joon Haeng Rhee (590461), Ju Young Lim (3391025), Choon-Mee Kim (3391022)   +3 more
core   +1 more source

Isoniazid-Resistance Conferring Mutations in Mycobacterium tuberculosis KatG: Catalase, Peroxidase, and INH-NADH Adduct Formation Activities

, 2009
Mycobacterium tuberculosis catalase-peroxidase (KatG) is a bifunctional hemoprotein which activates isoniazid (INH), a pro-drug that is integral to frontline antituberculosis treatments.
Cade, Christine Elizabeth
core  

Sensitivity of XcckatG to UV radiation.

, 2016
Exponential phase cultures of Xcc wild-type and katG mutant were exposed to the indicated doses of UV-A (A) and UV-B (B) radiation and the number of CFU after treatment was determined for each culture by plating of appropriate dilutions.
Ivana Kraiselburd (160345), María Verónica Fernández Zenoff (3175554), María Laura Tondo (152670), Elena G. Orellano (152678), María Eugenia Farías (3175551), María Laura Delprato (197228)   +5 more
core   +1 more source

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

, 2016
Mycobacterium tuberculosis (Mtb) KatG is a catalase−peroxidase that is thought to activate the antituberculosis drug isoniazid (INH). The local environment of Mtb KatG and its most prevalent INH-resistant mutant, KatG(S315T), is investigated with the ...
Richard S. Magliozzo (204160), Johannes P. M. Schelvis (2259751), Salem Chouchane (2695969), Xiangbo Zhao (2289805), Sofia M. Kapetanaki (2390857), Shengwei Yu (2289808)   +5 more
core   +1 more source

Catalase-peroxidase (KatG): a potential frontier in tuberculosis drug development

Critical Reviews in Biochemistry and Molecular Biology
Mycobacterium tuberculosis (Mtb) depends on the bifunctional enzyme catalase-peroxidase (KatG) for survival within the host. KatG exhibits both catalase and peroxidase activities, serving distinct yet critical roles. While its peroxidase activity is essential for activating the frontline tuberculosis drug isoniazid, its catalase activity protects Mtb ...
openaire   +3 more sources