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Improving the affinity and activity of CYP101D2 for hydrophobic substrates

Improving the affinity and activity of CYP101D2 for hydrophobic substrates

http://www.wikidata.org/entity/Q27681804

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Spectroscopic studies of the cytochrome P450 reaction mechanisms.The Oxidation of Hydrophobic Aromatic Substrates by Using a Variant of the P450 Monooxygenase CYP101B1.

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Improving the affinity and activity of CYP101D2 for hydrophobic substrates

http://www.wikidata.org/entity/Q27681804

description

2013 nî lūn-bûn

@nan

2013 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Improving the affinity and activity of CYP101D2 for hydrophobic substrates

@ast

Improving the affinity and activity of CYP101D2 for hydrophobic substrates

@en

Improving the affinity and activity of CYP101D2 for hydrophobic substrates

@nl

type

label

Improving the affinity and activity of CYP101D2 for hydrophobic substrates

@ast

Improving the affinity and activity of CYP101D2 for hydrophobic substrates

@en

Improving the affinity and activity of CYP101D2 for hydrophobic substrates

@nl

prefLabel

Improving the affinity and activity of CYP101D2 for hydrophobic substrates

@ast

Improving the affinity and activity of CYP101D2 for hydrophobic substrates

@en

Improving the affinity and activity of CYP101D2 for hydrophobic substrates

@nl

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Applied Microbiology and Biotechnology

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Improving the affinity and activity of CYP101D2 for hydrophobic substrates

@en

P2093

Alison Dale

http://www.w3.org/2001/XMLSchema#string

Luet-Lok Wong

http://www.w3.org/2001/XMLSchema#string

Weihong Zhou

http://www.w3.org/2001/XMLSchema#string

Wen Yang

http://www.w3.org/2001/XMLSchema#string

P2860

MolProbity: all-atom structure validation for macromolecular crystallography

Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate.

Processing of X-ray diffraction data collected in oscillation mode

Crystal structure of the F87W/Y96F/V247L mutant of cytochrome P-450cam with 1,3,5-trichlorobenzene bound and further protein engineering for the oxidation of pentachlorobenzene and hexachlorobenzene

Molecular recognition in (+)-alpha-pinene oxidation by cytochrome P450cam

An open conformation of mammalian cytochrome P450 2B4 at 1.6-A resolution

A role of the heme-7-propionate side chain in cytochrome P450cam as a gate for regulating the access of water molecules to the substrate-binding site

Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation

P450cam Visits an Open Conformation in the Absence of Substrate ,

Molecular Characterization of a Class I P450 Electron Transfer System from Novosphingobium aromaticivorans DSM12444

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3979-3990

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scholarly article

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10.1007/S00253-012-4278-7

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9

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97

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Stephen G. Bell

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1006574895

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22820521

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