FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD(P)H:flavin oxidoreductase.
about
Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:flavin adenine dinucleotide oxidoreductase (TftC) of Burkholderia cepacia AC1100Computational analysis of a novel mutation in ETFDH gene highlights its long-range effects on the FAD-binding motif.Complementarity of ensemble and single-molecule measures of protein motion: a relaxation dispersion NMR study of an enzyme complexIncreased catalytic efficiency following gene fusion of bifunctional methionine sulfoxide reductase enzymes from Shewanella oneidensisA novel 9-bp insertion detected in steroid 21-hydroxylase gene (CYP21A2): prediction of its structural and functional implications by computational methods.Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD.
P2860
FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD(P)H:flavin oxidoreductase.
description
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FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD
@nl
FAD is a preferred substrate a ...... NAD(P)H:flavin oxidoreductase.
@en
type
label
FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD
@nl
FAD is a preferred substrate a ...... NAD(P)H:flavin oxidoreductase.
@en
prefLabel
FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD
@nl
FAD is a preferred substrate a ...... NAD(P)H:flavin oxidoreductase.
@en
P2093
P2860
P356
P1476
FAD is a preferred substrate a ...... NAD(P)H:flavin oxidoreductase.
@en
P2093
Luying Xun
Pallop Karnchanaphanurach
Tai Man Louie
X Sunney Xie
P2860
P304
39450-39455
P356
10.1074/JBC.M206339200
P407
P577
2002-08-12T00:00:00Z