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

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Abstract

Then-alkane-assimilating yeastCandida maltosacontains several structurally related cytochromes P450 (P450) encoded by theCYP52multigene family, which are inducible by various long-chain hydrocarbons and fatty acids and which are responsible for the initial hydroxylation steps in the metabolism of these substrates. In the present work, the four majorn-alkane-inducibleC. maltosaP450 forms, CYP52A3, CYP52A4, CYP52A5, and CYP52A9, were enzymatically characterized, taking advantage of heterologous P450/reductase coexpression inSaccharomyces cerevisiae.Testing various alkanes and fatty acids, distinct preferences of the individual P450 forms concerning substrate class and chain length were detected, thus providing new insight into the functional diversity of theC. maltosaCYP52 family. Moreover, the results obtained emphasize these structurally related enzymes as a powerful tool for future studies on P450 structure-function relationships.

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    Citation Excerpt :

    Interestingly, multiple paralogs encoding P450s in the CYP52-family are present in the genomes of n-alkane-assimilating yeasts (Fig. 1B). The substrate specificities of a few of the CYP52-family P450s, mainly those in C. maltosa and C. tropicalis, have been examined; they were found to show distinct substrate preferences (Fig. 1B) (Eschenfeldt et al., 2003; Kim et al., 2007; Ohkuma et al., 1998; Van Bogaert et al., 2009; Zimmer et al., 1996). Some CYP52-family P450s showed strong substrate preferences for n-alkanes, whereas others showed strong preferences for the ω-terminal ends of fatty acids.

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1

Corresponding author, present address: Department of Biotechnology, University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113, Japan. Fax: +81-3-3812-9246. E-mail: [email protected].

2

Present address: Institute of Physical and Chemical Research, Wako-shi, Saitama, 351-01, Japan.

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