[Isolation and properties of NAD-dependent formate dehydrogenase from the yeast Candida methylica]

NAD-dependent formate dehydrogenase was purified from a cell-free extract of methanol-consuming yeast Candida methylica, using chromatography on DEAE-cellulose and gel-filtration on Sephadex G-200. The enzyme is electrophoretically homogeneous, consists of two identical subunits with molecular weight of 46,000 and is active within the pH range of 6-9; the Km values for NAD and formate are 1 . 10(-4) and 1,3 . 10(-2) M, respectively. Formate dehydrogenase is inhibited by p-chloromercurybenzoate, iodoacetate, dithionitrobenzoate and azide.