Role of protein flexibility in the catalytic cycle of p-hydroxybenzoate hydroxylase elucidated by the Pro293Ser mutant.
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Crystal structure of Bacteroides thetaiotaomicron TetX2: A tetracycline degrading monooxygenase at 2.8 Å resolutionMarked changes in electron transport through the blue copper protein azurin in the solid state upon deuterationForm follows function: structural and catalytic variation in the class a flavoprotein monooxygenases.Epoxyquinone formation catalyzed by a two-component flavin-dependent monooxygenase involved in biosynthesis of the antibiotic actinorhodin.Altered balance of half-reactions in p-hydroxybenzoate hydroxylase caused by substituting the 2'-carbon of FAD with fluorine.Kinetic Mechanisms of the Oxygenase from a Two-component Enzyme,p-Hydroxyphenylacetate 3-Hydroxylase fromAcinetobacter baumannii
P2860
Role of protein flexibility in the catalytic cycle of p-hydroxybenzoate hydroxylase elucidated by the Pro293Ser mutant.
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2002 nî lūn-bûn
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name
Role of protein flexibility in ...... dated by the Pro293Ser mutant.
@en
Role of protein flexibility in ...... dated by the Pro293Ser mutant.
@nl
type
label
Role of protein flexibility in ...... dated by the Pro293Ser mutant.
@en
Role of protein flexibility in ...... dated by the Pro293Ser mutant.
@nl
prefLabel
Role of protein flexibility in ...... dated by the Pro293Ser mutant.
@en
Role of protein flexibility in ...... dated by the Pro293Ser mutant.
@nl
P2093
P356
P1433
P1476
Role of protein flexibility in ...... dated by the Pro293Ser mutant.
@en
P2093
Barrie Entsch
David P Ballou
Kendra King Frederick
Rajit Basu
P304
P356
10.1021/BI012073G
P407
P50
P577
2002-07-01T00:00:00Z