The structure of CYP101D2 unveils a potential path for substrate entry into the active site
about
A novel type of allosteric regulation: functional cooperativity in monomeric proteinsStructural Analysis of Mammalian Cytochrome P450 2B4 Covalently Bound to the Mechanism-Based Inactivator tert -Butylphenylacetylene: Insight into Partial Enzymatic ActivityConformational Adaptation of Human Cytochrome P450 2B6 and Rabbit Cytochrome P450 2B4 Revealed upon Binding Multiple Amlodipine MoleculesStructure and function of CYP108D1 from Novosphingobium aromaticivorans DSM12444: an aromatic hydrocarbon-binding P450 enzymeP450cin Active Site Water: Implications for Substrate Binding and Solvent AccessibilityCrystal Structures and Functional Characterization of Wild-Type CYP101D1 and Its Active Site MutantsThe crystal structures of 4-methoxybenzoate bound CYP199A2 and CYP199A4: structural changes on substrate binding and the identification of an anion binding siteImproving the affinity and activity of CYP101D2 for hydrophobic substratesInvestigation of the substrate range of CYP199A4: modification of the partition between hydroxylation and desaturation activities by substrate and protein engineeringEnzyme-substrate complex structures of CYP154C5 shed light on its mode of highly selective steroid hydroxylationThe crystal structure of the versatile cytochrome P450 enzyme CYP109B1 from Bacillus subtilisA Comparative Analysis of the Effector Role of Redox Partner Binding in Bacterial P450s.Conformational Heterogeneity and the Affinity of Substrate Molecular Recognition by Cytochrome P450cam.X-ray crystal structure of cytochrome P450 monooxygenase CYP101J2 from Sphingobium yanoikuyae strain B2.Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX.The dynamics of camphor in the cytochrome P450 CYP101D2.Crystallization and preliminary X-ray analysis of CYP153C1 from Novosphingobium aromaticivorans DSM12444.The Oxidation of Hydrophobic Aromatic Substrates by Using a Variant of the P450 Monooxygenase CYP101B1.Ligand Access Channels in Cytochrome P450 Enzymes: A Review.
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The structure of CYP101D2 unveils a potential path for substrate entry into the active site
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年学术文章
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2011年学术文章
@zh-cn
2011年学术文章
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2011年学术文章
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2011年学术文章
@zh-sg
2011年學術文章
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name
The structure of CYP101D2 unve ...... ate entry into the active site
@ast
The structure of CYP101D2 unve ...... ate entry into the active site
@en
The structure of CYP101D2 unve ...... ate entry into the active site
@en-gb
The structure of CYP101D2 unve ...... ate entry into the active site
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type
label
The structure of CYP101D2 unve ...... ate entry into the active site
@ast
The structure of CYP101D2 unve ...... ate entry into the active site
@en
The structure of CYP101D2 unve ...... ate entry into the active site
@en-gb
The structure of CYP101D2 unve ...... ate entry into the active site
@nl
prefLabel
The structure of CYP101D2 unve ...... ate entry into the active site
@ast
The structure of CYP101D2 unve ...... ate entry into the active site
@en
The structure of CYP101D2 unve ...... ate entry into the active site
@en-gb
The structure of CYP101D2 unve ...... ate entry into the active site
@nl
P2093
P2860
P50
P356
P1433
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The structure of CYP101D2 unve ...... ate entry into the active site
@en
P2093
Luet-Lok Wong
Weihong Zhou
P2860
P356
10.1042/BJ20101017
P407
P577
2011-01-01T00:00:00Z