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Structure-analyses of KatG mutations imparting isoniazid resistance

, 2009
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Purification and characterization of Mycobacterium tuberculosis KatG, KatG(S315T), and Mycobacterium bovis KatG(R463L)

Protein Expression and Purification, 2004
Isoniazid, a first-line antibiotic used for the treatment of tuberculosis, is a prodrug that requires activation by the Mycobacterium tuberculosis enzyme KatG. The KatG(S315T) mutation causes isoniazid resistance while the KatG(R463L) variation is thought to be a polymorphism.
Nancy L, Wengenack, Brian D, Lane, Preston J, Hill, James R, Uhl, Gudrun S, Lukat-Rodgers, Leslie, Hall, Glenn D, Roberts, Franklin R, Cockerill, Patrick J, Brennan, Kenton R, Rodgers, John T, Belisle, Frank, Rusnak   +11 more
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Redox Thermodynamics of the Ferric−Ferrous Couple of Wild-Type Synechocystis KatG and KatG(Y249F)

Biochemistry, 2006
Crystal structures and mass spectrometric analyses of catalase-peroxidases (KatGs) from different organisms revealed the existence of a peculiar distal Met-Tyr-Trp cross-link. The adduct appears to be important for the catalase but not the peroxidase activity of bifunctional KatG.
BELLEI, Marzia, C. Jakopitsch, BATTISTUZZI, Gianantonio, SOLA, Marco, C. Obinger   +4 more
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Carbon Monoxide Adducts of KatG and KatG(S315T) as Probes of the Heme Site and Isoniazid Binding

Biochemistry, 2001
KatG, 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, N L, Wengenack, F, Rusnak, K R, Rodgers   +3 more
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Evidence for Differential Binding of Isoniazid byMycobacteriumtuberculosisKatG and the Isoniazid-Resistant Mutant KatG(S315T)

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, S, Todorovic, L, Yu, F, Rusnak   +3 more
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Stimulation of KatG catalase activity by peroxidatic electron donors

Archives of Biochemistry and Biophysics, 2012
Catalase-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, Robert L, Moore, Douglas C, Goodwin   +2 more
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Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7Å resolution

Journal of Molecular Biology, 2003
The 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 ...
Xavi, Carpena, Suvit, Loprasert, Skorn, Mongkolsuk, Jacek, Switala, Peter C, Loewen, Ignacio, Fita   +5 more
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Enhancing the peroxidatic activity of KatG by deletion mutagenesis

Journal of Inorganic Biochemistry, 2012
Catalase-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 N, Kudalkar, Robert A, Campbell, Yongjiang, Li, Cornelius L, Varnado, Corey, Prescott, Douglas C, Goodwin   +5 more
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Catalase-peroxidase (KatG) Structure and Function

2015
Catalase-peroxidases, or KatGs, are fascinating multifunctional enzymes the first of which, from Escherichia coli, was characterized in 1979. The first crystal structure of a KatG from Haloarcula morismortui was reported in 2002 as a homodimer in which the N- and C-terminal domains of each subunit are structurally very similar.
Ignacio Fita, Xavi Carpena, Peter C. Loewen   +2 more
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