The alkane-hydroxylating enzyme system of the yeast Candida guilliermondii.
The growth of the investigated Candida guilliermondii strain on n-alkanes induces an alkane-hydroxylating enzyme system, which consists of a cytochrome P-450 and a NADPH-dependent reductase. The cytochrome P-450 was purified to 4 nmoles per mg protein. Long-chain alkanes, preferably hexadecane to octadecane, are hydroxylated to the corresponding primary alcohol by this enzyme system. The substrate induces a type I spectrum, other compounds checked type II spectra.
D000473:Alkanes; D002175:Candida / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification / Q000378:metabolism*; D003579:Cytochrome Reductases / Q000032:analysis; D003580:Cytochromes / Q000032:analysis; D006900:Hydroxylation; D006899:Mixed Function Oxygenases / Q000032:analysis; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D009252:NADPH Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D009251:NADPH-Ferrihemoprotein Reductase / Q000032:analysis
D000473:Alkanes; D003580:Cytochromes; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009247:NADH, NADPH Oxidoreductases; D003579:Cytochrome Reductases; D009251:NADPH-Ferrihemoprotein Reductase; D009252:NADPH Dehydrogenase