ИСТИНА

Nowadays enzyme-catalyzed reactions play a great role in fine organic synthesis. One of the largest groups of such enzymes is oxidoredyctases. Many of them use NAD(P)H as a cofactor. That’s why a second enzyme for NAD(P)H regeneration is needed. One of the best candidates for such processes is formate dehydrogenase (FDH, EC 1.2.1.2.). It catalyses the reaction of formate oxidation to carbon dioxide coupled with reduction of NAD(P)+ to NAD(P)H. The main advantages of FDH are irreversibility of the process, low price of substrate – formate ion and wide pH optimum of activity. The gene, encoded FDH was found in different bacteria, yeasts, fungi and plants. Later the main attention was devoted to bacterial FDHs while now the enzymes from different sources such as fungi, plants and yeasts have been successfully studied. In our laboratory many genes encoded FDH were cloned and expressed in E.coli cells such as active and soluble enzymes. Also, we’ve got several 3D structures of holo and apo forms of the enzyme. The systematic study of FDHs properties revealed, that the most thermally stable are FDHs from bacteria, but FDHs from plants have the best kinetic properties. In the present work we tried to combine the best features of the enzymes from different sources and obtained several biocatalysts with excellent characteristics.