Kinetic Mechanisms of the Oxygenase from a Two-component Enzyme,p-Hydroxyphenylacetate 3-Hydroxylase fromAcinetobacter baumannii
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A flavin-dependent monooxygenase from Mycobacterium tuberculosis involved in cholesterol catabolismStructure of the monooxygenase component of a two-component flavoprotein monooxygenaseCrystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8Mechanism and regulation of the Two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolorThe oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer-Villiger monooxygenase.Multiple pathways guide oxygen diffusion into flavoenzyme active sites.Hydrogen peroxide elimination from C4a-hydroperoxyflavin in a flavoprotein oxidase occurs through a single proton transfer from flavin N5 to a peroxide leaving groupSingle-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics.Form follows function: structural and catalytic variation in the class a flavoprotein monooxygenases.The reaction kinetics of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1 provide an understanding of the para-hydroxylation enzyme catalytic cycle.Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA.Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase.pH-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase.The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain.Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms.
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P2860
Kinetic Mechanisms of the Oxygenase from a Two-component Enzyme,p-Hydroxyphenylacetate 3-Hydroxylase fromAcinetobacter baumannii
description
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
im April 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Journal of Biological Chemistry
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wetenschappelijk artikel
@nl
наукова стаття, опублікована у квітні 2006
@uk
name
Kinetic Mechanisms of the Oxyg ...... se fromAcinetobacter baumannii
@en
Kinetic Mechanisms of the Oxyg ...... se fromAcinetobacter baumannii
@nl
type
label
Kinetic Mechanisms of the Oxyg ...... se fromAcinetobacter baumannii
@en
Kinetic Mechanisms of the Oxyg ...... se fromAcinetobacter baumannii
@nl
prefLabel
Kinetic Mechanisms of the Oxyg ...... se fromAcinetobacter baumannii
@en
Kinetic Mechanisms of the Oxyg ...... se fromAcinetobacter baumannii
@nl
P2093
P2860
P356
P1476
Kinetic mechanisms of the oxyg ...... e from Acinetobacter baumannii
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P2093
Barrie Entsch
David P Ballou
Jeerus Sucharitakul
P2860
P304
17044-17053
P356
10.1074/JBC.M512385200
P407
P577
2006-04-20T00:00:00Z