Alkane oxidation by a particulate preparation from Candida.
The oxidation of decane by a cell-free particulate preparation from Candida intermedia was studied. Decane is oxidized to decanoate via decanol and decanaldehyde. Oxidation of decane to decanol requires molecular oxygen. Decanol is oxidized to decanaldehyde by a nicotinamide adenine dinucleotide-linked dehydrogenase differing greatly in specificity from ordinary yeast alcohol dehydrogenase. Decanaldehyde is oxidized to decanoate by a nicotinamide adenine dinucleotide-linked dehydrogenase that oxidizes long-chain aldehydes but not short-chain aldehydes. The enzymes that oxidize decane, decanol, and decanaldehyde are all induced when decane is present in the medium. These enzymes are apparently located in the cell membrane.
D000143:Acids / Q000096:biosynthesis; D000438:Alcohols / Q000096:biosynthesis; D000447:Aldehydes / Q000096:biosynthesis; D000473:Alkanes / Q000378:metabolism*; D002175:Candida / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism*; D002247:Carbon Isotopes; D002462:Cell Membrane / Q000201:enzymology; D002474:Cell-Free System; D002854:Chromatography, Paper; D003470:Culture Media; D006863:Hydrogen-Ion Concentration; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism; D010101:Oxygen Consumption; D013053:Spectrophotometry
D000143:Acids; D000438:Alcohols; D000447:Aldehydes; D000473:Alkanes; D002247:Carbon Isotopes; D003470:Culture Media; D009243:NAD; D010088:Oxidoreductases