Properties of enzymes from Clostridium thermoaceticum and Clostridium formicoaceticum

Abstract

Methylenetetrahydrofolate dehydrogenase from C. thermoaceticum and C. formicoaceticum have been purified to homogeneity and compared. The two enzymes are very similar physically, chemically, and kinetically, but he C. thermoaceticum enzyme has a higher thermostablility, which is an intrinsic property of the protein. Formate dehydrogenase enzymes from both bacteria require selenite and tungstate for formation and these enzymes also appear to have similar properties, although the C. thermoaceticum is stable at 70 degrees C for more than one hour. Acetate kinase from C. thermoaceticum appears to be under metabolic control. It can be concluded that enzymes from C. thermoaceticum, although they are more thermostable, are very similar to corresponding enzymes from mesophilic organisms.