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  • 1985-1989  (2)
  • 1900-1904
  • Candida maltosa  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 147 (1987), S. 240-244 
    ISSN: 1432-072X
    Keywords: Cytochrome P-450 ; Alkane hydroxylation ; Candida maltosa ; Carbon monoxide inhibition ; Oxygen limitation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A method for selective and reversible inhibition of the alkane hydroxylating cytochrome P-450 in growing yeast cells was developed. Using low concentrations of carbon monoxide in a specially adapted small-scale fermentor system a complete inhibition of the first step of alkane degradation was obtained, obviously without influencing further metabolic steps. Thus, fatty alcohols which were shown to be the immediate products of the cytochrome P-450 catalyzed reaction were utilized with unchanged rates by yeast cultures blocked with carbon monoxide in alkane degradation. Moreover, significant differences were found in the pO2-dependencies of utilization of n-alkanes, fatty alcohols and further intermediates. It was concluded, that the alkane hydroxylating cytochrome P-450 system is distinguished by the lowest oxygen affinity among the oxygen-activating enzyme systems involved in alkane assimilation.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 147 (1987), S. 245-248 
    ISSN: 1432-072X
    Keywords: Candida maltosa ; Cytochrome P-450 ; Alkane hydroxylation ; Oxygen-limitation ; Carbon monoxide-inhibition ; Enzyme regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Transition of n-hexadecane utilizing cultures of Candida maltosa to oxygen-limited growth caused an up to 6-fold increase of the cellular cytochrome P-450 content. Enhanced cytochrome P-450 formation required protein de novo synthesis and was not due to a change of the apo/holo-enzyme ratio as demonstrated by cycloheximide inhibition and immunological quantitation. The effect of low oxygen concentration (pO2=3–5%) was simulated by selective inhibition of alkane hydroxylation with carbon monoxide (at a pO2 of 70–75%). Enhanced cytochrome P-450 formation occurred even when a constant growth rate was maintained through utilization of a second non-repressive growth substrate. However, the presence of n-alkanes was an essential precondition. It was concluded, that the cytochrome P-450 formation was mainly regulated by the intracellular inducer concentration which depends on the relative rates of alkane transport into the cell and the actual alkane hydroxylating activity of the enzyme system.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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