Biotransformations using prokaryotic P450 monooxygenases.
Recent studies on microbial cytochrome P450 enzymes have covered several new areas. Advances have been made in structure-function analysis and new non-enzymatic/electrochemical systems for the replacement of NAD(P)H in biocatalysis have been developed. Furthermore, the properties of some enzymes have been re-engineered by site-directed mutagenesis or by methods of directed evolution and new P450s have been functionally expressed and characterized. It is thought that a combination of these approaches will facilitate the use of isolated P450 monooxygenases in biocatalysis.
Urlacher
Vlada
V
Institute for Technical Biochemistry, University of Stuttgart, Allmandring 31, D-70569, Stuttgart, Germany. itbvkha@po.uni-stuttgart.de
Schmid
Rolf D
RD
D001419:Bacteria / Q000201:enzymology* / Q000235:genetics*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019475:Camphor 5-Monooxygenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002384:Catalysis; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D044927:Electron-Transferring Flavoproteins; D005420:Flavoproteins; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D009251:NADPH-Ferrihemoprotein Reductase; D015202:Protein Engineering / Q000379:methods; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D044927:Electron-Transferring Flavoproteins; D005420:Flavoproteins; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D019475:Camphor 5-Monooxygenase; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases