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Molecular cloning and characterization of the primary structure of the alkane hydroxylating cytochrome P-450 from the yeast Candida maltosa

1989; Elsevier BV; Volume: 161; Issue: 2 Linguagem: Inglês

10.1016/0006-291x(89)92677-6

1090-2104

Wolf‐Hagen Schunck, Eva Kärgel, B Gross, Brigitte Wiedmann, Stephan Mauersberger, Katarina Kopke, U. Kießling, Mike Strauss, Matthias Gaestel, Hansgeorg Müller,

Photosynthetic Processes and Mechanisms

A cDNA library was established starting from poly(A) RNA of n-alkane-grown Candida maltosa cells and cDNA clones were isolated containing the entire coding sequence for the alkane hydroxylating cytochrome P-450. The deduced protein consists of 521 amino acids, contains two putative transmembrane segments in the N-terminal region and has a characteristic heme-binding sequence in the C-terminal part. Sequence alignments with members of 11 reported cytochrome P-450 families revealed a strong homology to an alkane-inducible cytochrome P-450 from Candida tropicalis.