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PRIMARY STRUCTURE OF THE CYTOCHROME P450 LANOSTEROL 14A-DEMETHYLASE GENE FROM CANDIDA TROPICALIS
Chen, C., V. F. Kalb, T. G. Turi, AND J. C. Loper. PRIMARY STRUCTURE OF THE CYTOCHROME P450 LANOSTEROL 14A-DEMETHYLASE GENE FROM CANDIDA TROPICALIS. DNA. Mary Ann Liebert, Inc., Larchmont, NY, 7(9):617-626, (1988).
We report the nucleotide sequence of the gene and flanking DNA for the cytochrome P450 lanosterol 14 alpha-demethylase (14DM) from the yeast Candida tropicalis ATCC750. An open reading frame (ORF) of 528 codons encoding a 60.9-kD protein is identified. This ORF includes a characteristic heme-binding domain, HR2, common to all P450 proteins. This protein and the 14DM from Saccharomyces cerevisiae share 66.5% identical and 23.1% conservatively replaced amino acids in a 516-amino-acid alignment, and thus are orthologous forms of the P450LIA1 gene. Conversely, C. tropicalis 14DM shares relatively little sequence similarity with P450alk, the predominant P450 protein present when this organism is grown on n-alkanes. Sequence information of these three yeast P450s will be useful for structure-function analyses in the future.