ИСТИНА

NAD+-dependent formate dehydrogenase (FDH) is a universal “enzyme of stress” in plants. Its content sharply increases during such conditions as drought, high ultraviolet irradiation dose, abrupt jumps of temperature, lack of oxygen or important microelements, pathogen infection, etc. As a result of formate dehedrogenase reaction NADH is formed and then it is involved in ATP synthesis. ATP is a source of energy, which is very important for the liquidation of stress consequence. Therefore, by increasing the activity of formate dehydrogenase in the plant cell, it would be possible to create plants, which can overcome stress aftereffects faster. The genes, encoded recombinant formate dehydrogenases from soy Glycine max and Arabidopsis thaliana were successfully cloned in E. coli cells and as a result enzymes SoyFDH and AthFDH were obtained in active and soluble forms. The enzyme from soya is an object of great interests due to its best Michaelis constants both for substrate and coenzyme among all studied FDHs from different other sources. The structure of SoyFDH was analyzed and several mutant forms of the enzyme with improved properties were obtained. Thermal stability and catalytic activity were dramatically improved by single-point mutation. This work was supported by Russian Foundation for Basic Research, (projects 11-04-00920-a and 12-04-31740-а).