Document Detail

Lack of regio- and stereospecificity in oxidation of (+) camphor by Streptomyces griseus enriched in cytochrome P-450soy.
MedLine Citation:
PMID:  2116789     Owner:  NLM     Status:  MEDLINE    
Oxidation of (+) camphor by cytochrome P-450soy-enriched intact cells of Streptomyces griseus resulted in the formation of one major and several minor metabolites. The minor metabolites were identified as 3-endo-hydroxycamphor (2%), 5-endo-hydroxycamphor (7%), 5-exo-hydroxycamphor (9%), 2,5-diketobornane (2%), and camphorquinone (3%). The major metabolite was isolated and conclusively identified as 6-endo-hydroxycamphor (60%). When supplemented with NADPH, spinach ferredoxin:NADP oxidoreductase and spinach ferredoxin, homogeneous preparations of cytochrome P-450soy oxidized camphor to a mixture of 3-endo-, 5-endo-, 5-exo-and 6-endo-hydroxycamphor. The data presented indicates that cytochrome P-450soy resembles its mammalian counterparts in its lack of regio- and stereospecificity in camphor oxidation.
F S Sariaslani; L R McGee; M K Trower; F G Kitson
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  170     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1990 Jul 
Date Detail:
Created Date:  1990-09-10     Completed Date:  1990-09-10     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  456-61     Citation Subset:  IM    
Central Research and Development Department, E. I. duPont de Nemours & Company, Wilmington, DE 19880-0228.
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MeSH Terms
Camphor / metabolism*
Cytochrome P-450 Enzyme System / metabolism
Oxidoreductases / metabolism
Soybeans / enzymology
Streptomyces griseus / enzymology,  growth & development,  metabolism*
Reg. No./Substance:
76-22-2/Camphor; 9035-51-2/Cytochrome P-450 Enzyme System; EC 1.-/Oxidoreductases; EC reductase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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