Metabolism of alkane by yeast

We demonstrated two NAD⁺-linked alcohol dehydrogenases in cell free extracts ofCandida tropicalis grown onn-tetradecane. Comparative studies of localization, properties and regulation indicate that these enzymes are involved in two different pathways ofn-alkane metabolism, one cytoplasmic and the other mitochondrial. Kinetic properties, such as the variation of the K_m and V_max as a function of substrate chain length of the soluble NAD⁺-linked alcohol dehydrogenase, might involve hydrophobic interactions between the substrate and the enzyme. One of five papers being published from the Symposium “Biochemistry of Hydrocarbon Degradation,” presented at the AOCS Meeting, Chicago, September 1970.