215 related articles for article (PubMed ID: 17188362)
1. Modification of the active site of Mycobacterium tuberculosis KatG after disruption of the Met-Tyr-Trp cross-linked adduct.
Kapetanaki SM; Zhao X; Yu S; Magliozzo RS; Schelvis JP
J Inorg Biochem; 2007 Mar; 101(3):422-33. PubMed ID: 17188362
[TBL] [Abstract][Full Text] [Related]
2. Conformational differences in Mycobacterium tuberculosis catalase-peroxidase KatG and its S315T mutant revealed by resonance Raman spectroscopy.
Kapetanaki S; Chouchane S; Girotto S; Yu S; Magliozzo RS; Schelvis JP
Biochemistry; 2003 Apr; 42(13):3835-45. PubMed ID: 12667074
[TBL] [Abstract][Full Text] [Related]
3. Mycobacterium tuberculosis KatG(S315T) catalase-peroxidase retains all active site properties for proper catalytic function.
Kapetanaki SM; Chouchane S; Yu S; Zhao X; Magliozzo RS; Schelvis JP
Biochemistry; 2005 Jan; 44(1):243-52. PubMed ID: 15628865
[TBL] [Abstract][Full Text] [Related]
4. Role of the oxyferrous heme intermediate and distal side adduct radical in the catalase activity of Mycobacterium tuberculosis KatG revealed by the W107F mutant.
Zhao X; Yu S; Ranguelova K; Suarez J; Metlitsky L; Schelvis JP; Magliozzo RS
J Biol Chem; 2009 Mar; 284(11):7030-7. PubMed ID: 19139098
[TBL] [Abstract][Full Text] [Related]
5. The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties.
Ghiladi RA; Knudsen GM; Medzihradszky KF; Ortiz de Montellano PR
J Biol Chem; 2005 Jun; 280(24):22651-63. PubMed ID: 15840564
[TBL] [Abstract][Full Text] [Related]
6. Radical sites in Mycobacterium tuberculosis KatG identified using electron paramagnetic resonance spectroscopy, the three-dimensional crystal structure, and electron transfer couplings.
Ranguelova K; Girotto S; Gerfen GJ; Yu S; Suarez J; Metlitsky L; Magliozzo RS
J Biol Chem; 2007 Mar; 282(9):6255-64. PubMed ID: 17204474
[TBL] [Abstract][Full Text] [Related]
7. Isoniazid-resistance conferring mutations in Mycobacterium tuberculosis KatG: catalase, peroxidase, and INH-NADH adduct formation activities.
Cade CE; Dlouhy AC; Medzihradszky KF; Salas-Castillo SP; Ghiladi RA
Protein Sci; 2010 Mar; 19(3):458-74. PubMed ID: 20054829
[TBL] [Abstract][Full Text] [Related]
8. Carbon monoxide adducts of KatG and KatG(S315T) as probes of the heme site and isoniazid binding.
Lukat-Rodgers GS; Wengenack NL; Rusnak F; Rodgers KR
Biochemistry; 2001 Jun; 40(24):7149-57. PubMed ID: 11401561
[TBL] [Abstract][Full Text] [Related]
9. Rapid formation of compound II and a tyrosyl radical in the Y229F mutant of Mycobacterium tuberculosis catalase-peroxidase disrupts catalase but not peroxidase function.
Yu S; Girotto S; Zhao X; Magliozzo RS
J Biol Chem; 2003 Nov; 278(45):44121-7. PubMed ID: 12944408
[TBL] [Abstract][Full Text] [Related]
10. Mutation of katG in a clinical isolate of Mycobacterium tuberculosis: effects on catalase-peroxidase for isoniazid activation.
Purkan ; Ihsanawati ; Natalia D; Syah YM; Retnoningrum DS; Kusuma HS
Ukr Biochem J; 2016; 88(5):71-81. PubMed ID: 29235814
[TBL] [Abstract][Full Text] [Related]
11. Three-dimensional model and molecular mechanism of Mycobacterium tuberculosis catalase-peroxidase (KatG) and isoniazid-resistant KatG mutants.
Mo L; Zhang W; Wang J; Weng XH; Chen S; Shao LY; Pang MY; Chen ZW
Microb Drug Resist; 2004; 10(4):269-79. PubMed ID: 15650370
[TBL] [Abstract][Full Text] [Related]
12. A radical on the Met-Tyr-Trp modification required for catalase activity in catalase-peroxidase is established by isotopic labeling and site-directed mutagenesis.
Zhao X; Suarez J; Khajo A; Yu S; Metlitsky L; Magliozzo RS
J Am Chem Soc; 2010 Jun; 132(24):8268-9. PubMed ID: 20507091
[TBL] [Abstract][Full Text] [Related]
13. Role of the Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG) as revealed by KatG(M255I).
Ghiladi RA; Medzihradszky KF; Ortiz de Montellano PR
Biochemistry; 2005 Nov; 44(46):15093-105. PubMed ID: 16285713
[TBL] [Abstract][Full Text] [Related]
14. The crystal structure of isoniazid-bound KatG catalase-peroxidase from Synechococcus elongatus PCC7942.
Kamachi S; Hirabayashi K; Tamoi M; Shigeoka S; Tada T; Wada K
FEBS J; 2015 Jan; 282(1):54-64. PubMed ID: 25303560
[TBL] [Abstract][Full Text] [Related]
15. Two [Fe(IV)=O Trp*] intermediates in M. tuberculosis catalase-peroxidase discriminated by multifrequency (9-285 GHz) EPR spectroscopy: reactivity toward isoniazid.
Singh R; Switala J; Loewen PC; Ivancich A
J Am Chem Soc; 2007 Dec; 129(51):15954-63. PubMed ID: 18052167
[TBL] [Abstract][Full Text] [Related]
16. Antibiotic resistance in Mycobacterium tuberculosis: peroxidase intermediate bypass causes poor isoniazid activation by the S315G mutant of M. tuberculosis catalase-peroxidase (KatG).
Suarez J; Ranguelova K; Schelvis JPM; Magliozzo RS
J Biol Chem; 2009 Jun; 284(24):16146-16155. PubMed ID: 19363028
[TBL] [Abstract][Full Text] [Related]
17. Catalase in peroxidase clothing: Interdependent cooperation of two cofactors in the catalytic versatility of KatG.
Njuma OJ; Ndontsa EN; Goodwin DC
Arch Biochem Biophys; 2014 Feb; 544():27-39. PubMed ID: 24280274
[TBL] [Abstract][Full Text] [Related]
18. An oxyferrous heme/protein-based radical intermediate is catalytically competent in the catalase reaction of Mycobacterium tuberculosis catalase-peroxidase (KatG).
Suarez J; Ranguelova K; Jarzecki AA; Manzerova J; Krymov V; Zhao X; Yu S; Metlitsky L; Gerfen GJ; Magliozzo RS
J Biol Chem; 2009 Mar; 284(11):7017-29. PubMed ID: 19139099
[TBL] [Abstract][Full Text] [Related]
19. Molecular Analysis of
Purkan P; Ihsanawati I; Natalia D; Syah YM; Retnoningrum DS; Siswanto I
J Med Life; 2018; 11(2):160-167. PubMed ID: 30140323
[TBL] [Abstract][Full Text] [Related]
20. Reduced affinity for Isoniazid in the S315T mutant of Mycobacterium tuberculosis KatG is a key factor in antibiotic resistance.
Yu S; Girotto S; Lee C; Magliozzo RS
J Biol Chem; 2003 Apr; 278(17):14769-75. PubMed ID: 12586821
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]