Rapid formation of compound II and a tyrosyl radical in the Y229F mutant of Mycobacterium tuberculosis catalase-peroxidase disrupts catalase but not peroxidase function.
about
An oxyferrous heme/protein-based radical intermediate is catalytically competent in the catalase reaction of Mycobacterium tuberculosis catalase-peroxidase (KatG)Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazidCrystal structure of Mycobacterium tuberculosis catalase-peroxidaseIsoniazid-resistance conferring mutations in Mycobacterium tuberculosis KatG: catalase, peroxidase, and INH-NADH adduct formation activitiesDetection of multidrug resistance in Mycobacterium tuberculosisModification of the active site of Mycobacterium tuberculosis KatG after disruption of the Met-Tyr-Trp cross-linked adduct.Radical sites in Mycobacterium tuberculosis KatG identified using electron paramagnetic resonance spectroscopy, the three-dimensional crystal structure, and electron transfer couplingsSpecific function of the Met-Tyr-Trp adduct radical and residues Arg-418 and Asp-137 in the atypical catalase reaction of catalase-peroxidase KatGMauG: a di-heme enzyme required for methylamine dehydrogenase maturation.Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase.A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidasesA radical on the Met-Tyr-Trp modification required for catalase activity in catalase-peroxidase is established by isotopic labeling and site-directed mutagenesisRole of the oxyferrous heme intermediate and distal side adduct radical in the catalase activity of Mycobacterium tuberculosis KatG revealed by the W107F mutant.Evidence for radical formation at Tyr-353 in Mycobacterium tuberculosis catalase-peroxidase (KatG).Catalase-peroxidases (KatG) exhibit NADH oxidase activity.Influence of the unusual covalent adduct on the kinetics and formation of radical intermediates in synechocystis catalase peroxidase: a stopped-flow and EPR characterization of the MET275, TYR249, and ARG439 variants.Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron hole-hopping within the enzyme.The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties.
P2860
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P2860
Rapid formation of compound II and a tyrosyl radical in the Y229F mutant of Mycobacterium tuberculosis catalase-peroxidase disrupts catalase but not peroxidase function.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Rapid formation of compound II ...... e but not peroxidase function.
@en
Rapid formation of compound II ...... e but not peroxidase function.
@nl
type
label
Rapid formation of compound II ...... e but not peroxidase function.
@en
Rapid formation of compound II ...... e but not peroxidase function.
@nl
prefLabel
Rapid formation of compound II ...... e but not peroxidase function.
@en
Rapid formation of compound II ...... e but not peroxidase function.
@nl
P2093
P2860
P356
P1476
Rapid formation of compound II ...... e but not peroxidase function.
@en
P2093
Richard S Magliozzo
Shengwei Yu
Stefania Girotto
Xiangbo Zhao
P2860
P304
44121-44127
P356
10.1074/JBC.M304757200
P407
P577
2003-08-27T00:00:00Z