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Comparative studies of localization, properties and regulation indicate that these enzymes are involved in two different pathways of<jats:italic>n<\/jats:italic>\u2010alkane metabolism, one cytoplasmic and the other mitochondrial. Kinetic properties, such as the variation of the K<jats:sub>m<\/jats:sub> and V<jats:sub>max<\/jats:sub> as a function of substrate chain length of the soluble NAD<jats:sup>+<\/jats:sup>\u2010linked alcohol dehydrogenase, might involve hydrophobic interactions between the substrate and the enzyme.<\/jats:p>","DOI":"10.1007\/bf02531226","type":"journal-article","created":{"date-parts":[[2006,11,21]],"date-time":"2006-11-21T06:00:38Z","timestamp":1164088838000},"page":"444-447","source":"Crossref","is-referenced-by-count":14,"title":["Metabolism of alkane by yeast"],"prefix":"10.1002","volume":"6","author":[{"given":"J. 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