A new Bacillus megaterium whole-cell catalyst for the hydroxylation of the pentacyclic triterpene 11-keto-β-boswellic acid (KBA) based on a recombinant cytochrome P450 system

2011 ◽  
Vol 93 (3) ◽  
pp. 1135-1146 ◽  
Author(s):  
Sabrina Bleif ◽  
Frank Hannemann ◽  
Josef Zapp ◽  
David Hartmann ◽  
Johann Jauch ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Bacillus Megaterium ◽  
Boswellic Acid ◽  
Pentacyclic Triterpene ◽  
Whole Cell ◽  
Cytochrome P450 System

A new cytochrome P450 system from Bacillus megaterium DSM319 for the hydroxylation of 11-keto-β-boswellic acid (KBA)

2013 ◽  
Vol 98 (4) ◽  
pp. 1703-1717 ◽  
Author(s):  
Elisa Brill ◽  
Frank Hannemann ◽  
Josef Zapp ◽  
Gerit Brüning ◽  
Johann Jauch ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Bacillus Megaterium ◽  
Boswellic Acid ◽  
Cytochrome P450 System

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.

Construction and Functional Analysis of Mycolicibacterium smegmatis Recombinant Strains Carrying the Genes of Bacillary Cytochromes CYP106A1 and CYP106A2

2021 ◽  
Vol 37 (6) ◽  
pp. 34-47
Author(s):  
V.M. Nikolaeva ◽  
V.V. Fokina ◽  
A.A. Shutov ◽  
A.V. Kazantsev ◽  
N.I. Strizhov ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Heterologous Expression ◽  
Bacillus Megaterium ◽  
Cytochromes P450 ◽  
Maximum Level ◽  
13C Nmr Spectroscopy ◽  
Cytochrome P450 Monooxygenases ◽  
Russian Science ◽  
Steroid Nucleus ◽  
Recombinant Strains

Mycolicibacterium smegmatis mc2155 has been genetically modified to be used as a platform for the expression of foreign cytochrome P450 monooxygenases by introducing deletions in the kshB and kstD genes that encode key stages of the enzymatic destruction of the steroid nucleus. Three sets of genetic constructs have been created for heterologous expression of the genes of cytochromes P450 CYP106A1 from Bacillus megaterium DSM319 and CYP106A2 from Bacillus megaterium ATCC13368 in Mycolicibacterium smegmatis mc2155 (ΔkshBΔkstD) cells. The recombinant plasmids contained monocistronic expression cassettes of cytochrome genes (NS31 and pNS32), or tricistronic cassettes of cytochrome genes together with cDNA copies of adrenodoxin and andrenodoxin reductase genes of the bovine adrenal cortex (pNS33 and pNS34), or monocistronic gene cassettes of chimeric cytochromes fused with the DNA sequence encoding the CYP116B2 reductase domain from the soil bacterium Rhodococcus sp. NCIMB 9784 (pNS35 and pNS36). The recombinant strains of mycolicibacteria were shown to selectively monohydroxylate androstenedione (AD) under growth conditions. The product was identified as 15-hydroxyandrostenedione (15-OH-AD) by mass spectrometry and 1H and 13C NMR spectroscopy. The maximum level of 15-OH-AD production (17.3 ± 1.5 mg/L) was observed when using the recombinant M. smegmatis mc2155 (ΔkshBΔkstD) (pNS32) strain, which expresses a single cyp106A2 gene from B. megaterium ATCC13368. Host proteins of M. smegmatis mc2155 were shown to be capable of supplying electrons to heterologous cytochromes to support their hydroxylating activity. The results are of priority character, expand the understanding of the hydroxylation of steroid compounds by bacterial cytochromes CYP106A1/A2 and are important for the creation of microbial strains producing valuable hydroxysteroids. cyp106A1, cyp106A2, cytochrome P450, heterologous expression, Bacillus megaterium, Mycolicibacterium smegmatis, 15β-hydroxylation, bioconversion, steroids This work was supported by the Russian Science Foundation (project No. 21-64-00024).

The Renal Cytochrome P450 System Generates Novel Arachidonic Acid Metabolites

1989 ◽  
pp. 109-129 ◽  
Author(s):  
Michal Schwartzman ◽  
Mairead A. Carroll ◽  
David Sacerdoti ◽  
Nader G. Abraham ◽  
John C. McGiff
Keyword(s):  
Arachidonic Acid ◽  
Cytochrome P450 ◽  
Cytochrome P450 System ◽  
Arachidonic Acid Metabolites ◽  
Acid Metabolites

Whole-cell amperometric biosensor for screening of cytochrome P450 inhibitors

2016 ◽  
Vol 223 ◽  
pp. 392-399 ◽  
Author(s):  
Tal Yoetz-Kopelman ◽  
Carmit Porat-Ophir ◽  
Yosi Shacham-Diamand ◽  
Amihay Freeman
Keyword(s):  
Cytochrome P450 ◽  
Amperometric Biosensor ◽  
Whole Cell ◽  
P450 Inhibitors
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