Progress towards the easier use of P450 enzymes.
The cytochrome P450 enzymes (P450s or CYPs) form a large family of heme proteins involved in drug metabolism and in the biosynthesis of steroids, lipids, vitamins and natural products. Their remarkable ability to catalyze the insertion of oxygen into non-activated C-H bonds has attracted the interest of chemists for several decades. Very few chemical methods exist that directly hydroxylate aliphatic or aromatic C-H bonds, and most of them are not selective or of limited scope. Biocatalysts such as P450s represent a promising alternative: however, their applications have been limited by substrate specificity, low activity, poor stability and the need for cofactors. This review covers the attempts to overcome these limitations using approaches such as mutagenesis, chemical modifications, conditions engineering and immobilization.
Chefson
Amandine
A
Department of Chemistry, McGill University, 801 Sherbrooke Street West, Montréal, Québec, Canada H3A 2K6.
Auclair
Karine
K
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics*; D019475:Camphor 5-Monooxygenase / Q000737:chemistry / Q000235:genetics*; D002384:Catalysis; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000235:genetics*; D004795:Enzyme Stability; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000235:genetics*; D008954:Models, Biological; D015394:Molecular Structure; D016296:Mutagenesis; D009251:NADPH-Ferrihemoprotein Reductase; D015202:Protein Engineering / Q000379:methods*; D012997:Solvents / Q000494:pharmacology; D013379:Substrate Specificity
D001426:Bacterial Proteins; D012997:Solvents; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D019475:Camphor 5-Monooxygenase; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases