Origins of the diversity of cytochrome P450 CYP74 family based on the results of site-directed mutagenesis.

Autor: Toporkova, Ya., Mukhtarova, L., Gogolev, Yu., Grechkin, A.
Zdroj: Moscow University Biological Sciences Bulletin; Dec2010, Vol. 65 Issue 4, p155-157, 3p
Abstrakt: Bioinformatic analysis and site-directed mutagenesis allowed identification of the determinants of catalysis for CYP74, which are located in the central part of the I-helix and ERR triad. Mutations K302S and T366Y in tomato allene oxide syntase LeAOS3 induced possession of hydroperoxide lyase activity. In contrast to the wild-type MtHPL enzyme that produces C-aldoacid, mutant forms F284I, F287V, G288I, N285A, and N285T of alfalfa hydroperoxide lyase MtHPL synthesized C- and C-fragments. Our data provide evidence that the CYP74 family originated from a common ancestor with hydroperoxide lyase activity. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
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