Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444 - Wikidata - wikimedia - TriplyDB

Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

http://www.wikidata.org/entity/Q27666374

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Metals in biology: defining metalloproteomes Structural Analysis of Mammalian Cytochrome P450 2B4 Covalently Bound to the Mechanism-Based Inactivator tert -Butylphenylacetylene: Insight into Partial Enzymatic Activity Structure and function of CYP108D1 from Novosphingobium aromaticivorans DSM12444: an aromatic hydrocarbon-binding P450 enzyme Solution Structural Ensembles of Substrate-Free Cytochrome P450 cam The crystal structures of 4-methoxybenzoate bound CYP199A2 and CYP199A4: structural changes on substrate binding and the identification of an anion binding site Improving the affinity and activity of CYP101D2 for hydrophobic substrates The crystal structure of the versatile cytochrome P450 enzyme CYP109B1 from Bacillus subtilis Selective oxidation of carotenoid-derived aroma compounds by CYP260B1 and CYP267B1 from Sorangium cellulosum So ce56.X-ray crystal structure of cytochrome P450 monooxygenase CYP101J2 from Sphingobium yanoikuyae strain B2.Crystallization and preliminary X-ray analysis of CYP153C1 from Novosphingobium aromaticivorans DSM12444.Sesquiterpenoids from the herb of Leonurus japonicus.The Oxidation of Hydrophobic Aromatic Substrates by Using a Variant of the P450 Monooxygenase CYP101B1.Engineering of the cytochrome P450 monooxygenase system for benzyl maltol hydroxylation.CYP109E1 is a novel versatile statin and terpene oxidase from Bacillus megaterium.

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

http://www.wikidata.org/entity/Q27666374

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2011 nî lūn-bûn

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2011 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2011 թվականի հունվարին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

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Luet-Lok Wong

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Ming Ma

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Nicholas H Rees

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Weihong Zhou

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Wen Yang

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

Yiming Hao

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

Zihe Rao

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Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone

The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin

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

The catalytic pathway of cytochrome p450cam at atomic resolution

Probing the open state of cytochrome P450cam with ruthenium-linker substrates

Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies

Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 A resolution: evidence for multiple substrate binding modes

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

Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry

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88-99

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scholarly article

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10.1002/CBIC.201000537

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1

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12

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Stephen G. Bell

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2011-01-03T00:00:00Z

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49680321

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21154803

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