Metabolic conditions determining the composition and catalytic activity of cytochrome P-450 monooxygenases in Candida tropicalis

Details

Serval ID
serval:BIB_D5481A920830
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Metabolic conditions determining the composition and catalytic activity of cytochrome P-450 monooxygenases in Candida tropicalis
Journal
Journal of Bacteriology
Author(s)
Sanglard  D., Kappeli  O., Fiechter  A.
ISSN
0021-9193 (Print)
Publication state
Published
Issued date
01/1984
Volume
157
Number
1
Pages
297-302
Notes
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jan
Abstract
In the microsomal fraction of Candida tropicalis cells, two distinct monooxygenases were detected, depending on the growth conditions. The distinction of the two monooxygenases was evident from: (i) the absorption maxima in the reduced CO difference spectra of the terminal oxidases (cytochromes P-450 and P-448); (ii) the contents of the monooxygenase components (cytochromes P-450/P-448, NADPH-cytochrome c (P-450) reductase, and cytochrome b5) and (iii) the catalytic activity of the complete system (aliphatic hydroxylation and N-demethylation activity). The occurrence of the respective monooxygenases could be related to the carbon source (n-alkanes or glucose). Oxygen limitation led to a significant increase of cytochrome P-450/P-448 content, independent of the carbon source utilized by the cells. An improved method for the isolation of microsomes enabled us to demonstrate the presence of cytochrome P-448 in glucose-grown cells.
Keywords
Alkanes/metabolism Candida/analysis/*enzymology Catalysis Culture Media/metabolism Cytochrome P-450 Enzyme System Cytochromes/analysis Glucose/metabolism Microsomes/analysis/enzymology Oxygenases/analysis/*metabolism
Pubmed
Web of science
Create date
25/01/2008 14:40
Last modification date
20/08/2019 15:55
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