Results 181 to 190 of about 8,860 (214)
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Enhancing the Peroxidatic Activity of KatG by Deletion Mutagenesis
Journal of Inorganic Biochemistry, 2012Catalase-peroxidase (KatG) enzymes use a peroxidase active site to facilitate robust catalase activity, an ability all other members of its superfamily lack. KatG's have a Met-Tyr-Trp covalent adduct that is essential for catalatic but not peroxidatic turnover. The tyrosine (Y226 in E.
Shalley Kudalkar +2 more
exaly +3 more sources
Catalase-Peroxidase KatG of Burkholderia pseudomallei at 1.7 Å Resolution
Journal of Molecular Biology, 2003The catalase-peroxidase encoded by katG of Burkholderia pseudomallei (BpKatG) is 65% identical with KatG of Mycobacterium tuberculosis, the enzyme responsible for the activation of isoniazid as an antibiotic. The structure of a complex of BpKatG with an unidentified ligand, has been solved and refined at 1.7A resolution using X-ray synchrotron data ...
Suvit Loprasert +2 more
exaly +3 more sources
Carbon Monoxide Adducts of KatG and KatG(S315T) as Probes of the Heme Site and Isoniazid Binding
Biochemistry, 2001KatG, the catalase peroxidase from Mycobacterium tuberculosis, is important in the activation of the antitubercular drug, isoniazid. About 50% of isoniazid-resistant clinical isolates contain a mutation in KatG wherein the serine at position 315 is substituted with threonine, KatG(S315T).
G S, Lukat-Rodgers +3 more
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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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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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Biochemistry, 1998
Isoniazid is a mainstay of antibiotic therapy for the treatment of tuberculosis, but its molecular mechanism of action is unclear. Previous investigators have hypothesized that isoniazid is a prodrug that requires in vivo activation by KatG, the catalase-peroxidase of Mycobacterium tuberculosis, and that resistance to isoniazid strongly correlates with
N L, Wengenack +3 more
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Isoniazid is a mainstay of antibiotic therapy for the treatment of tuberculosis, but its molecular mechanism of action is unclear. Previous investigators have hypothesized that isoniazid is a prodrug that requires in vivo activation by KatG, the catalase-peroxidase of Mycobacterium tuberculosis, and that resistance to isoniazid strongly correlates with
N L, Wengenack +3 more
openaire +2 more sources
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
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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Stimulation of KatG catalase activity by peroxidatic electron donors
Archives of Biochemistry and Biophysics, 2012Catalase-peroxidases (KatGs) use a peroxidase scaffold to support robust catalase activity, an ability no other member of its superfamily possesses. Because catalase turnover requires H(2)O(2) oxidation, whereas peroxidase turnover requires oxidation of an exogenous electron donor, it has been anticipated that the latter should inhibit catalase ...
Elizabeth N, Ndontsa +2 more
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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
openaire +2 more sources