scholarly journals Characterization of P450 FcpC, the Enzyme Responsible for Bioconversion of Diosgenone to Isonuatigenone in Streptomyces virginiae IBL-14

2009 ◽  
Vol 75 (12) ◽  
pp. 4202-4205 ◽  
Author(s):  
Wei Wang ◽  
Feng-Qing Wang ◽  
Dong-Zhi Wei
Keyword(s):  
Escherichia Coli ◽  
Electron Transfer ◽  
Cytochrome P450 ◽  
Cytochrome P450 Monooxygenase ◽  
P450 Monooxygenase ◽  
Whole Cell ◽  
Electron Transfer Chain ◽  
Streptomyces Virginiae ◽  
Transfer Chain

ABSTRACT A new cytochrome P450 monooxygenase, FcpC, from Streptomyces virginiae IBL-14 has been identified. This enzyme is found to be responsible for the bioconversion of a pyrano-spiro steroid (diosgenone) to a rare nuatigenin-type spiro steroid (isonuatigenone), which is a novel C-25-hydroxylated diosgenone derivative. A whole-cell P450 system was developed for the production of isonuatigenone via the expression of the complete three-component electron transfer chain in an Escherichia coli strain.

scholarly journals Characterization of cytochrome P450 monooxygenase CYP154H1 from the thermophilic soil bacterium Thermobifida fusca

2010 ◽  
Vol 89 (5) ◽  
pp. 1475-1485 ◽  
Author(s):  
Anett Schallmey ◽  
Gijs den Besten ◽  
Ite G. P. Teune ◽  
Roga F. Kembaren ◽  
Dick B. Janssen
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Monooxygenase ◽  
Soil Bacterium ◽  
Thermobifida Fusca ◽  
P450 Monooxygenase

scholarly journals Characterization of the cytochrome P450 monooxygenase genes (P450ome) from the carotenogenic yeast Xanthophyllomyces dendrorhous

BMC Genomics ◽  
2017 ◽  
Vol 18 (1) ◽  
Author(s):  
Pamela Córdova ◽  
Ana-María Gonzalez ◽  
David R. Nelson ◽  
María-Soledad Gutiérrez ◽  
Marcelo Baeza ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Monooxygenase ◽  
Xanthophyllomyces Dendrorhous ◽  
P450 Monooxygenase

scholarly journals Biocatalytic Conversion of Avermectin to 4"-Oxo-Avermectin: Characterization of Biocatalytically Active Bacterial Strains and of Cytochrome P450 Monooxygenase Enzymes and Their Genes

2005 ◽  
Vol 71 (11) ◽  
pp. 6968-6976 ◽  
Author(s):  
Volker Jungmann ◽  
István Molnár ◽  
Philip E. Hammer ◽  
D. Steven Hill ◽  
Ross Zirkle ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cytochrome P450 ◽  
Recombinant Proteins ◽  
Oxidation Reaction ◽  
Cytochrome P450 Monooxygenases ◽  
Enzyme Kinetic ◽  
Bacterial Strains ◽  
P450 Monooxygenase ◽  
P450 Monooxygenases

ABSTRACT 4"-Oxo-avermectin is a key intermediate in the manufacture of the agriculturally important insecticide emamectin benzoate from the natural product avermectin. Seventeen biocatalytically active Streptomyces strains with the ability to oxidize avermectin to 4"-oxo-avermectin in a regioselective manner have been discovered in a screen of 3,334 microorganisms. The enzymes responsible for this oxidation reaction in these biocatalytically active strains were found to be cytochrome P450 monooxygenases (CYPs) and were termed Ema1 to Ema17. The genes for Ema1 to Ema17 have been cloned, sequenced, and compared to reveal a new subfamily of CYPs. Ema1 to Ema16 have been overexpressed in Escherichia coli and purified as His-tagged recombinant proteins, and their basic enzyme kinetic parameters have been determined.

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