Active site structure and substrate specificity of cytochrome P450 4A1 : Steric control of ligand approach perpendicular to heme plane

Biochemical and Biophysical Research Communications

Volumn 219, Issue 2, 1996, Pages 445-449

  Bambal, Ramesh B ^a   Hanzlik, Robert P ^a  

^a UNIVERSITY OF KANSAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLENE DERIVATIVE; ALKENE DERIVATIVE; AROMATIC COMPOUND; CYTOCHROME P450; ENZYME INHIBITOR; HEME; HYBRID PROTEIN; LAURIC ACID; NONANOIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE FERRIHEMOPROTEIN REDUCTASE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITOR INTERACTION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROXYLATION; MOLECULAR MODEL; PRIORITY JOURNAL; STEREOSPECIFICITY;

ALKANE 1-MONOOXYGENASE; ALLOSTERIC REGULATION; BINDING SITES; CYTOCHROME P-450 ENZYME SYSTEM; DICARBOXYLIC ACIDS; FATTY ACIDS, MONOUNSATURATED; FATTY ACIDS, UNSATURATED; HEME; KINETICS; LAURIC ACIDS; LIGANDS; MIXED FUNCTION OXYGENASES; RECOMBINANT FUSION PROTEINS; SUBSTRATE SPECIFICITY;

EID: 0029983833     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1996.0253     Document Type: Article

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