Functional expression of the cholesterol side-chain cleavage cytochrome P450scc systemстатья
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Аннотация:The alkane-utilizing yeast Y. lipolytica was tested as an alternative host for P450-catalyzed biotransformation of steroids or sterols. Inducible functional expression of the ER-resident P450c17 (bovine CYP17A1 cDNA, 17alpha-hydroxylase) in Y. lipolytica was investigated in comparison with the yeast Saccharomyces cerevisiae. The P450c17 expressed was found to be highly activein alkane-growing Y. lipolytica cells, catalyzing the biotransformation of progesterone into 17alpha-hydroxyprogesterone, indicating significant advantages of this hydrophobic compounds-utilizing yeast as a host to perform P450-catalyzed bioconversion reactions with hydrophobic substrates (Applied Biochemistry Microbiology 42: 472; Biochemistry (Moscow) 74:1482). The construction of new recombinant Y. lipolytica strains for functional expression of the cholesterol side-chain cleavage P450scc system (human CYP11A1, Adx, AdR) together with P450c17 will be presented. The applied method for recombinant strain construction is obviously a useful tool for the heterologous expression of multi-component P450 enzyme systems in Y. lipolytica. Supported by INTAS (CA-03-51-4366), BRFFI (B04IC-030), RFFI (05-04-48049-a)