Switching pyridine nucleotide specificity in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes.
about
Crystal structure analysis of Bacillus subtilis ferredoxin-NADP+ oxidoreductase and the structural basis for its substrate selectivityThe crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3Variations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamilyModulation of the enzymatic efficiency of ferredoxin-NADP(H) reductase by the amino acid volume around the catalytic site.Cytochrome P450/redox partner fusion enzymes: biotechnological and toxicological prospects.P450(BM3) (CYP102A1): connecting the dots.High-resolution studies of hydride transfer in the ferredoxin:NADP+ reductase superfamily.Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP(+) oxidoreductase activity toward NADPH.Fusion to Hydrophobin HFBI Improves the Catalytic Performance of a Cytochrome P450 System.Characterisation of the flavin adenine dinucleotide binding region of Myxococcus xanthus protoporphyrinogen oxidase.Improved product-per-glucose yields in P450-dependent propane biotransformations using engineered Escherichia coli.C-terminal tail residue Arg1400 enables NADPH to regulate electron transfer in neuronal nitric-oxide synthase.Analysis of the interactions of cytochrome b5 with flavocytochrome P450 BM3 and its domains.Kinetic analysis of cytochrome P450 reductase from Artemisia annua reveals accelerated rates of NADH-dependent flavin reduction.Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3.Aromatic substitution of the FAD-shielding tryptophan reveals its differential role in regulating electron flux in methionine synthase reductase and cytochrome P450 reductase.
P2860
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P2860
Switching pyridine nucleotide specificity in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
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2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
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2005年學術文章
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2005年學術文章
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name
Switching pyridine nucleotide ...... the W1046H and W1046A enzymes.
@en
Switching pyridine nucleotide ...... the W1046H and W1046A enzymes.
@nl
type
label
Switching pyridine nucleotide ...... the W1046H and W1046A enzymes.
@en
Switching pyridine nucleotide ...... the W1046H and W1046A enzymes.
@nl
prefLabel
Switching pyridine nucleotide ...... the W1046H and W1046A enzymes.
@en
Switching pyridine nucleotide ...... the W1046H and W1046A enzymes.
@nl
P2093
P2860
P356
P1476
Switching pyridine nucleotide ...... the W1046H and W1046A enzymes.
@en
P2093
Andrew W Munro
Nigel S Scrutton
Olivier Roitel
Rajasekhar Neeli
P2860
P304
17634-17644
P356
10.1074/JBC.M413826200
P407
P577
2005-02-14T00:00:00Z