Preparative use of isolated CYP102 monooxygenases -- a critical appraisal.
Isolated P450 monooxygenases have for long been neglected catalysts in enzyme technology. This is surprising as they display a remarkable substrate specificity catalyzing reactions, which represent a challenge for classic organic chemistry. On the other hand, many P450 monooxygenases are membrane bound, depend on rather complicated electron transfer systems and require expensive cofactors such as NAD(P)H. Their activities are low, and stability leaves much to be desired. The use of bacterial P450 monooxygenases from CYP102 family allows overcoming some of these handicaps. They are soluble and their turnovers are high, presumably because their N-terminal heme monooxygenase and their C-terminal diflavin reductase domain are covalently linked. In recent years, protein engineering approaches have been successfully used to turn CYP102 monooxgenases into powerful biocatalysts.
Eiben
Sabine
S
Institute of Technical Biochemistry, Allmandring 31, D-70569 Stuttgart, Germany.
Kaysser
Leonard
L
Maurer
Steffen
S
Kühnel
Katja
K
Urlacher
Vlada B
VB
Schmid
Rolf D
RD
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D002384:Catalysis; D003067:Coenzymes / Q000737:chemistry*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism; D004795:Enzyme Stability; D007218:Industrial Microbiology / Q000379:methods; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism; D009251:NADPH-Ferrihemoprotein Reductase; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D001426:Bacterial Proteins; D003067:Coenzymes; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; C445019:CYP102A3 protein, Bacillus subtilis; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases