Purification and characterization of recombinant catalase-peroxidase, which confers isoniazid sensitivity in Mycobacterium tuberculosis
about
Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr.The tuberculosis prodrug isoniazid bound to activating peroxidasesCrystal structure of Mycobacterium tuberculosis catalase-peroxidaseIdentification of arylamine N-acetyltransferase inhibitors as an approach towards novel anti-tubercularsKinetic and spectroscopic characterization of a hydroperoxy compound in the reaction of native myoglobin with hydrogen peroxide.Mycobacterial catalase-peroxidase is a tissue antigen and target of the adaptive immune response in systemic sarcoidosis.S-nitroso proteome of Mycobacterium tuberculosis: Enzymes of intermediary metabolism and antioxidant defense.Identification of katG mutations associated with high-level isoniazid resistance in Mycobacterium tuberculosis.Isoniazid-resistance conferring mutations in Mycobacterium tuberculosis KatG: catalase, peroxidase, and INH-NADH adduct formation activitiesEnzyme-catalyzed mechanism of isoniazid activation in class I and class III peroxidases.Exploring the structure and function of the mycobacterial KatG protein using trans-dominant mutants.Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenaseDetection of multidrug resistance in Mycobacterium tuberculosisAntibiotic resistance in Mycobacterium tuberculosis: peroxidase intermediate bypass causes poor isoniazid activation by the S315G mutant of M. tuberculosis catalase-peroxidase (KatG)Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803: cloning, overexpression in Escherichia coli, and kinetic characterization.A radical on the Met-Tyr-Trp modification required for catalase activity in catalase-peroxidase is established by isotopic labeling and site-directed mutagenesisEvidence for radical formation at Tyr-353 in Mycobacterium tuberculosis catalase-peroxidase (KatG).Catalase reaction by myoglobin mutants and native catalase: mechanistic investigation by kinetic isotope effect.Relationship between mutation of serine residue at 315th position in M. tuberculosis catalase-peroxidase enzyme and Isoniazid susceptibility: an in silico analysis.KatG reduces H2O2Plant sulfite oxidase as novel producer of H2O2: combination of enzyme catalysis with a subsequent non-enzymatic reaction step.Effect of Distal Cavity Mutations on the Formation of Compound I in Catalase-Peroxidases
P2860
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P2860
Purification and characterization of recombinant catalase-peroxidase, which confers isoniazid sensitivity in Mycobacterium tuberculosis
description
1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1997
@ast
im Dezember 1997 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1997/12/12)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/12/12)
@nl
наукова стаття, опублікована в грудні 1997
@uk
name
Purification and characterizat ...... in Mycobacterium tuberculosis
@ast
Purification and characterizat ...... in Mycobacterium tuberculosis
@en
Purification and characterizat ...... in Mycobacterium tuberculosis
@nl
type
label
Purification and characterizat ...... in Mycobacterium tuberculosis
@ast
Purification and characterizat ...... in Mycobacterium tuberculosis
@en
Purification and characterizat ...... in Mycobacterium tuberculosis
@nl
prefLabel
Purification and characterizat ...... in Mycobacterium tuberculosis
@ast
Purification and characterizat ...... in Mycobacterium tuberculosis
@en
Purification and characterizat ...... in Mycobacterium tuberculosis
@nl
P2093
P2860
P356
P1476
Purification and characterizat ...... in Mycobacterium tuberculosis
@en
P2093
A. E. Cass
J. M. Nagy
K. A. Brown
P2860
P304
31265–31271
P356
10.1074/JBC.272.50.31265
P407
P577
1997-12-12T00:00:00Z