Biochemistry (Mosc). 2004 Nov, v. 69, N11, p.1252-67(Engl), 1537-1554(Rus).
Catalytic mechanism and
application of formate dehydrogenase.
Tishkov VI*,
Popov VO.
*Department of Chemical Enzymology, Faculty of
Chemistry, Lomonosov Moscow State University, Moscow, 119992, Russia.
vit@enz.chem.msu.ru.
NAD+-dependent formate dehydrogenase (FDH)
is an abundant enzyme that plays an important role in energy supply of
methylotrophic microorganisms and in response to stress in plants. FDH
belongs to the superfamily of D-specific 2-hydroxy acid dehydrogenases.
FDH is widely accepted as a model enzyme to study the mechanism of
hydride ion transfer in the active center of dehydrogenases because the
reaction catalyzed by the enzyme is devoid of proton transfer steps and
implies a substrate with relatively simple structure. FDH is also widely
used in enzymatic syntheses of optically active compounds as a versatile
biocatalyst for NAD(P)H regeneration consumed in the main reaction. This
review covers the late developments in cloning genes of FDH from various
sources, studies of its catalytic mechanism and physiological role, and
its application for new chiral syntheses.
