Engineering Bacterial Cytochrome P450 Bm3 into a Prototype with Human P450 Enzyme Activity Using Indigo Formation
نویسندگان
چکیده
School of Biological Sciences and Technology, Chonnam National University, Gwangju 500757, Republic of Korea (S.-H.P., Do.-H.K., Da.-H.K., C.-H.Y.); Systems Microbiology Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305806, Republic of Korea (Doo.K., H.-C.J., J.-G.P.); Department of Biochemistry, College of Veterinary Medicine, Chonnam National University, Gwangju 500-757, Republic of Korea (T.A); Department of Biological Sciences, Konkuk University, Seoul, 413-701, Republic of Korea (Don.K.) DMD Fast Forward. Published on January 25, 2010 as doi:10.1124/dmd.109.030759
منابع مشابه
Engineering bacterial cytochrome P450 (P450) BM3 into a prototype with human P450 enzyme activity using indigo formation.
Human cytochrome P450 (P450) enzymes metabolize a variety of endogenous and xenobiotic compounds, including steroids, drugs, and environmental chemicals. In this study, we examine the possibility that bacterial P450 BM3 (CYP102A1) mutants with indole oxidation activity have the catalytic activities of human P450 enzymes. Error-prone polymerase chain reaction was carried out on the heme domain-c...
متن کاملFormation of flavin semiquinone during the reduction of P450 BM3 reductase domain with NADPH.
Cytochrome P450 BM3 (P450 102) from Bacillus megaterium is a unique bacterial P450, formed from the fusion of a fatty acid hydroxylase to a eukaryotic-like NADPH-cytochrome P450 reductase flavoprotein in a single (1 19 kDa) polypeptide chain (1, 2). It is an attractive model system for enzymological and structural studies due to its homology with mammalian drug metabolising P450 systems, and wi...
متن کاملFormation of indigo by recombinant mammalian cytochrome P450.
The development of bicistronic systems for coexpression of recombinant human cytochrome P450 enzymes (P450s) with their redox partner, NADPH-cytochrome P450 reductase (NPR), has enabled P450 activity to be reconstituted within bacterial cells. During expression of recombinant P450 2E1 and some other forms, we observed the formation of a blue pigment in bacterial cultures. The pigment was extrac...
متن کاملFlavocytochrome P450 BM3: an update on structure and mechanism of a biotechnologically important enzyme.
Since its discovery in the 1980s, the fatty acid hydroxylase flavocytochrome P450 (cytochrome P450) BM3 (CYP102A1) from Bacillus megaterium has been adopted as a paradigm for the understanding of structure and mechanism in the P450 superfamily of enzymes. P450 BM3 was the first P450 discovered as a fusion to its redox partner--a eukaryotic-like diflavin reductase. This fact fuelled the interest...
متن کاملOptimization of the Bacterial Cytochrome P450 BM3 System for the Production of Human Drug Metabolites
Drug metabolism in human liver is a process involving many different enzymes. Among them, a number of cytochromes P450 isoforms catalyze the oxidation of most of the drugs commercially available. Each P450 isoform acts on more than one drug, and one drug may be oxidized by more than one enzyme. As a result, multiple products may be obtained from the same drug, and as the metabolites can be biol...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2010