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Metabolism of alkane by yeast
Author(s) -
Lebeault J. M.,
Azoulay E.
Publication year - 1971
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02531226
Subject(s) - alkane , nad+ kinase , candida tropicalis , biochemistry , yeast , enzyme , alcohol dehydrogenase , substrate (aquarium) , metabolism , tetradecane , chemistry , biology , stereochemistry , organic chemistry , catalysis , ecology
We demonstrated two NAD + ‐linked alcohol dehydrogenases in cell free extracts of Candida tropicalis grown on n ‐tetradecane. Comparative studies of localization, properties and regulation indicate that these enzymes are involved in two different pathways of n ‐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.