Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase.
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How pH Modulates the Reactivity and Selectivity of a Siderophore-Associated Flavin MonooxygenaseCrystallization and preliminary X-ray analysis of the reductase component of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii.The reaction kinetics of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1 provide an understanding of the para-hydroxylation enzyme catalytic cycle.The substrate oxidation mechanism of pyranose 2-oxidase and other related enzymes in the glucose-methanol-choline superfamily.Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA.Oxidation mode of pyranose 2-oxidase is controlled by pH.The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain.Selectivity of substrate binding and ionization of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase.Oxidative dehalogenation and denitration by a flavin-dependent monooxygenase is controlled by substrate deprotonationTyr217 and His213 are important for substrate binding and hydroxylation of 3-hydroxybenzoate 6-hydroxylase fromRhodococcus jostiiRHA1
P2860
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P2860
Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Interactions with the substrat ...... xyphenylacetate 3-hydroxylase.
@en
type
label
Interactions with the substrat ...... xyphenylacetate 3-hydroxylase.
@en
prefLabel
Interactions with the substrat ...... xyphenylacetate 3-hydroxylase.
@en
P2093
P2860
P356
P1476
Interactions with the substrat ...... xyphenylacetate 3-hydroxylase.
@en
P2093
Chanakan Tongsook
Jeerus Sucharitakul
Kittisak Thotsaporn
P2860
P304
44491-44502
P356
10.1074/JBC.M111.284463
P407
P577
2011-11-03T00:00:00Z