Role of a mutated residue at the entrance of the substrate access channel in cytochrome P450 engineered for vitamin D 3 hydroxylation activity

Biochemistry

Volumn 50, Issue 39, 2011, Pages 8302-8310

  Fukunishi, Hiroaki ^a   Yagi, Hirotaka ^a   Kamijo, Kenichi ^a   Shimada, Jiro ^a  

^a NEC CORPORATION   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING FREE ENERGY; BINDING POCKETS; BOUND STATE; COMPUTATIONAL APPROACH; CRYSTAL STRUCTURE ANALYSIS; CYTOCHROME P450; FUTURE CHALLENGES; INTERACTION FORCES; MD SIMULATION; MOLECULAR DYNAMICS SIMULATIONS; PROTEIN DATA BANK; QUANTUM CHEMICAL CALCULATIONS; SALT BRIDGES; STEERED MOLECULAR DYNAMICS; STRUCTURAL CHANGE; THREE DIMENSIONAL COORDINATE; VITAMIN-D; WILD-TYPE ENZYMES;

BINDING ENERGY; DYNAMICS; ENZYMES; HYDROXYLATION; MOLECULAR DYNAMICS; PORPHYRINS; QUANTUM CHEMISTRY; SUBSTRATES; VEHICULAR TUNNELS;

CRYSTAL STRUCTURE;

COLECALCIFEROL; CYTOCHROME P450; ENZYME; HEME;

ARTICLE; BINDING KINETICS; BIOENGINEERING; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; HYDROXYLATION; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MUTATION; PRIORITY JOURNAL; SIMULATION;

BINDING SITES; CHOLECALCIFEROL; CYTOCHROME P-450 ENZYME SYSTEM; HYDROXYLATION; MOLECULAR DYNAMICS SIMULATION; MUTATION; STEROID HYDROXYLASES; THERMODYNAMICS;

EID: 80053426513     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2006493     Document Type: Article

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