Document Detail

Characterization of the versatile monooxygenase CYP109B1 from Bacillus subtilis.
MedLine Citation:
PMID:  20186410     Owner:  NLM     Status:  MEDLINE    
The oxidizing activity of CYP109B1 from Bacillus subtilis was reconstituted in vitro with various artificial redox proteins including putidaredoxin reductase and putidaredoxin from Pseudomonas putida, truncated bovine adrenodoxin reductase and adrenodoxin, flavodoxin reductase and flavodoxin from Escherichia coli, and two flavodoxins from B. subtilis (YkuN and YkuP). Binding and oxidation of a broad range of chemically different substrates (fatty acids, n-alkanes, primary n-alcohols, terpenoids like (+)-valencene, alpha- and beta-ionone, and the steroid testosterone) were investigated. CYP109B1was found to oxidize saturated fatty acids (conversion up to 99%) and their methyl and ethyl esters (conversion up to 80%) at subterminal positions with a preference for the carbon atoms C11 and C12 counted from the carboxyl group. For the hydroxylation of primary n-alcohols, the omega(-2) position was preferred. n-Alkanes were not accepted as substrates by CYP109B1. Regioselective hydroxylation of terpenoids alpha-ionone (approximately 70% conversion) and beta-ionone (approximately 91% conversion) yielded the allylic alcohols 3-hydroxy-alpha-ionone and 4-hydroxy-beta-ionone, respectively. Furthermore, indole was demonstrated to inhibit fatty acid oxidation.
Marco Girhard; Tobias Klaus; Yogan Khatri; Rita Bernhardt; Vlada B Urlacher
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-02-26
Journal Detail:
Title:  Applied microbiology and biotechnology     Volume:  87     ISSN:  1432-0614     ISO Abbreviation:  Appl. Microbiol. Biotechnol.     Publication Date:  2010 Jun 
Date Detail:
Created Date:  2010-05-24     Completed Date:  2010-09-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8406612     Medline TA:  Appl Microbiol Biotechnol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  595-607     Citation Subset:  IM    
Institute of Technical Biochemistry, Universitaet Stuttgart, Allmandring 31, 70569, Stuttgart, Germany.
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MeSH Terms
Alcohols / chemistry,  metabolism
Alkanes / chemistry,  metabolism
Amino Acid Sequence
Bacillus subtilis / chemistry,  enzymology*,  genetics
Bacterial Proteins / chemistry*,  genetics,  isolation & purification,  metabolism
Cytochrome P-450 Enzyme System / chemistry*,  genetics,  isolation & purification,  metabolism
Enzyme Stability
Fatty Acids / chemistry,  metabolism
Molecular Sequence Data
Norisoprenoids / chemistry,  metabolism
Sequence Homology, Amino Acid
Substrate Specificity
Reg. No./Substance:
0/Alcohols; 0/Alkanes; 0/Bacterial Proteins; 0/Fatty Acids; 0/Norisoprenoids; 9035-51-2/Cytochrome P-450 Enzyme System

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