Separate enzymes catalyze the final two steps of coenzyme A biosynthesis in Brevibacterium ammoniagenes: purification of pantetheine phosphate adenylyltransferase.

We have discovered that the final two steps in coenzyme A biosynthesis in Brevibacterium ammoniagenes are catalyzed by distinct enzymes, readily separated by DEAE sepharose anion exchange chromatography. This is in contrast to mammalian tissues in which these two reactions are catalyzed by a single bifunctional enzyme (Worrall, D.M., and Tubbs, P.K. (1983) Biochem. J. 215, 153-157) and Bakers yeast in which these two activities have been identified as part of a multifunctional complex (Bucovaz, E.T., Rhoades, J.L., and Tarnowski, S.J. (1980) Fed. Proc. 39 (6), 142). The pantetheine phosphate adenylyltransferase has been purified to homogeneity and found to exist as a trimeric protein of molecular mass approximately 108 kDa. Of other nucleoside triphosphates tested as substrates, only 2'-deoxy-ATP showed measurable activity, being 27% that of ATP.