作者: Thomas Zimmer , Moriya Ohkuma , Akinori Ohta , Masamichi Takagi , Wolf-Hagen Schunck
关键词: Heterologous 、 Enzyme 、 Saccharomyces cerevisiae 、 Metabolism 、 Enzyme inducer 、 Yeast 、 Biochemistry 、 Hydroxylation 、 Biology 、 Genetics 、 Reductase 、 Biophysics 、 Cell biology 、 Molecular biology
摘要: The n-alkane-assimilating yeast Candida maltosa contains several structurally related cytochromes P450 (P450) encoded by the CYP52 multigene family, which are inducible various long-chain hydrocarbons and fatty acids responsible for initial hydroxylation steps in metabolism of these substrates. In present work, four major n-alkane-inducible C. forms; CYP52A3, CYP52A4, CYP52A5, CYP52A9, were enzymatically characterized, taking advantage heterologous P450/reductase coexpression Saccharomyces cerevisiae. Testing alkanes acids, distinct preferences individual forms concerning substrate class chain length detected, thus providing new insight into functional diversity family. Moreover, results obtained emphasize enzymes as a powerful tool future studies on structure-function relationships.