Abstract
A kinetic analysis of NAD-dependent formate dehydrogenase from methylotrophic bacteria, strain no. 1, has been carried out. Initial velocity, product, and dead-end inhibition studies are compatible with the rapid-equilibrium random kinetic mechanism. Chemical modification studies of formate dehydrogenase reveal essential cysteine and arginine residues. The influence of enzyme inactivation on the modification of hystidine and lysine residues was also investigated. The model of the enzyme active centre is proposed. Some practical applications of formate dehydrogenase are discussed.
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