TheCYP52Multigene Family ofCandida maltosaEncodes Functionally Diversen-Alkane-Inducible Cytochromes P450

作者: Thomas Zimmer , Moriya Ohkuma , Akinori Ohta , Masamichi Takagi , Wolf-Hagen Schunck

DOI: 10.1006/BBRC.1996.1100

关键词: HeterologousEnzymeSaccharomyces cerevisiaeMetabolismEnzyme inducerYeastBiochemistryHydroxylationBiologyGeneticsReductaseBiophysicsCell biologyMolecular 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.

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