HYPOTHETICAL OF THE CYP74 FAMILY OF CYTOCHROMES P450 DIVERSITY BASED ON RESULTS OF SITE-DIRECTED MUTAGENESIS
https://doi.org/10.1234/XXXX-XXXX-2010-4-29-32
Abstract
Bioinformatics analyses and site-directed mutagenesis enabled us to identify determinants of catalysis by CYP74 family enzymes in I-helix central domain and ERR-triad. Substitutions K302S and T366Y in tomato allene oxide synthase LeAOS3 led to hydroperoxide lyase activity appearance. Mutant forms F284I, F287V, G288I, N285A and N285T of alfalfa hydroperoxide lyase MtHPL, unlike wild-type enzyme produced predominantly 02-aldoacid, synthesized С13- and СИ-frag- ments. The data obtained confirm the evolutionary origin of CYP74 family diversity from a common ancestor with hydroperoxide lyase activity.
About the Authors
Ya. Yu. ToporkovaRussian Federation
L. Sh. Muchtarova,
Russian Federation
Yu. V. Gogolev
Russian Federation
A. N. Grechkin
Russian Federation
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Review
For citations:
Toporkova Ya.Yu., Muchtarova, L.Sh., Gogolev Yu.V., Grechkin A.N. HYPOTHETICAL OF THE CYP74 FAMILY OF CYTOCHROMES P450 DIVERSITY BASED ON RESULTS OF SITE-DIRECTED MUTAGENESIS. Vestnik Moskovskogo universiteta. Seriya 16. Biologiya. 2010;(4):29-32. (In Russ.) https://doi.org/10.1234/XXXX-XXXX-2010-4-29-32