Mechanism and role of covalent heme binding in the CYP4 family of P450 enzymes and the mammalian peroxidases

Drug Metabolism Reviews

Volumn 40, Issue 3, 2008, Pages 405-426

  Ortiz De Montellano, Paul R ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

CYP4A; CYP4B; CYP4F; Cytochrome P450; Eosinophil peroxidase; Fatty acid hydroxylation; Heme covalent attachment; Heme oxidation; Horseradish peroxidase; Hypohalide reactions; Lactoperoxidase; Myeloperoxidase; Thyroid peroxidase

Indexed keywords

CYTOCHROME P450; CYTOCHROME P450 4A; CYTOCHROME P450 4B; CYTOCHROME P450 4F; EOSINOPHIL PEROXIDASE; HEME; HORSERADISH PEROXIDASE; LACTOPEROXIDASE; METHIONINE; MYELOPEROXIDASE; PEROXIDASE; SULFONIUM DERIVATIVE; THYROID PEROXIDASE;

COVALENT BOND; ENZYME ACTIVE SITE; ENZYME MECHANISM; HUMAN; HYDROXYLATION; NONHUMAN; OXIDATION; REVIEW;

ALKANE 1-MONOOXYGENASE; ANIMALS; ARYL HYDROCARBON HYDROXYLASES; BINDING SITES; CYTOCHROME P-450 ENZYME SYSTEM; FATTY ACIDS; HEME; HUMANS; HYDROXYLATION; ISOENZYMES; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PEROXIDASES; PROTEIN BINDING; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 47649104479     PISSN: 03602532     EISSN: 10979883     Source Type: Journal    
DOI: 10.1080/03602530802186439     Document Type: Review

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