Results 231 to 240 of about 12,768 (245)
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Probing the structure and bifunctionality of catalase-peroxidase (KatG)
Journal of Inorganic Biochemistry, 2006Catalase-peroxidases (KatGs) exhibit peroxidase and substantial catalase activities similar to monofunctional catalases. Crystal structures of four different KatGs reveal the presence of a peroxidase-conserved proximal and distal heme pocket together with features unique to KatG.
SMULEVICH, GIULIETTA +3 more
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Biochemistry, 2005
Catalase-peroxidases (KatGs) are bifunctional enzymes possessing both catalase and peroxidase activities. Four crystal structures of different KatGs revealed the presence of a novel Met-Tyr-Trp cross-link which has been suggested to impart catalatic activity to the KatGs. To decipher the individual roles of the two cross-links in the Met-Tyr-Trp adduct,
Reza A, Ghiladi +2 more
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Catalase-peroxidases (KatGs) are bifunctional enzymes possessing both catalase and peroxidase activities. Four crystal structures of different KatGs revealed the presence of a novel Met-Tyr-Trp cross-link which has been suggested to impart catalatic activity to the KatGs. To decipher the individual roles of the two cross-links in the Met-Tyr-Trp adduct,
Reza A, Ghiladi +2 more
openaire +2 more sources
Biochemistry, 2001
The antitubercular agent isoniazid can be activated by Mycobacterium tuberculosis KatG using either a peroxidase compound I/II or a superoxide-dependent oxyferrous pathway. The identity of activated isoniazid is unknown, but it has been suggested that it may be a free radical intermediate.
N L, Wengenack, F, Rusnak
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The antitubercular agent isoniazid can be activated by Mycobacterium tuberculosis KatG using either a peroxidase compound I/II or a superoxide-dependent oxyferrous pathway. The identity of activated isoniazid is unknown, but it has been suggested that it may be a free radical intermediate.
N L, Wengenack, F, Rusnak
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Strain variation in the katG region of Mycobacterium tuberculosis
Molecular Microbiology, 1994SummarySouthern blot analysis of chromosomal DNA from clinical isolates of Mycobacterium tuberculosis using cosmid DNA probes revealed extensive strain variation in the katG region of the genome. In addition to deletion of the katG gene itself in some isoniazid‐resistant strains, adjacent DNA fragments were missing or altered in a range of drug ...
Y, Zhang, D, Young
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Molecular diversity of katG genes in the soil bacteria Comamonas
Archives of Microbiology, 2010Three complete katG genes coding for bifunctional catalase-peroxidases (KatGs) from the beta-proteobacterium Comamonas terrigena and two related strains of Comamonas testosteroni have been cloned and sequenced. Catalase-peroxidases are unique bifunctional enzymes known to be expressed in these soil bacteria in response to environmental and/or oxidative
Jana, Godocíková +4 more
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KATG: Keyword-Bias-Aware Adversarial Text Generation for Text Classification
Proceedings of the AAAI Conference on Artificial Intelligence, 2022Recent work has shown that current text classification models are vulnerable to small adversarial perturbation to inputs, and adversarial training that re-trains the models with the support of adversarial examples is the most popular way to alleviate the impact of the perturbation.
Lingfeng Shen, Shoushan Li, Ying Chen
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Catalase-Peroxidase (Mycobacterium tuberculosis KatG) Catalysis and Isoniazid Activation
Biochemistry, 2000Resonance Raman spectra of native, overexpressed M. tuberculosis catalase-peroxidase (KatG), the enzyme responsible for activation of the antituberculosis antibiotic isoniazid (isonicotinic acid hydrazide), have confirmed that the heme iron in the resting (ferric) enzyme is high-spin five-coordinate.
S, Chouchane, I, Lippai, R S, Magliozzo
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Biochemistry, 2000
Mycobacterium tuberculosis KatG is a multifunctional heme enzyme responsible for activation of the antibiotic isoniazid. A KatG(S315T) point mutation is found in >50% of isoniazid-resistant clinical isolates. Since isoniazid activation is thought to involve an oxidation reaction, the redox potential of KatG was determined using cyclic voltammetry ...
N L, Wengenack +7 more
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Mycobacterium tuberculosis KatG is a multifunctional heme enzyme responsible for activation of the antibiotic isoniazid. A KatG(S315T) point mutation is found in >50% of isoniazid-resistant clinical isolates. Since isoniazid activation is thought to involve an oxidation reaction, the redox potential of KatG was determined using cyclic voltammetry ...
N L, Wengenack +7 more
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Superoxide Reactivity of KatG: Insights into Isoniazid Resistance Pathways in TB
Journal of the American Chemical Society, 2004To gain insight into the mechanism of INH activation by KatG and to understand how resistance is conferred by the single active-site point mutation of KatG(S315T), we have employed pulse radiolysis as the means to initiate a catalytic pathway capable of mimicking the in vivo oxidation of isoniazid (INH).
Reza A, Ghiladi +2 more
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The Mycobacterium tuberculosis katG promoter region contains a novel upstream activator
Microbiology, 1999An Escherichia coli-mycobacterial shuttle vector, pJCluc, containing a luciferase reporter gene, was constructed and used to analyse the Mycobacterium tuberculosis katG promoter. A 1.9 kb region immediately upstream of katG promoted expression of the luciferase gene in E. coli and Mycobacterium smegmatis.
Michelle A, Mulder +2 more
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