CoASAc-independent Phosphoenolpyruvate Carboxylase from an Obligate Methylotroph Hyphomicrobium methylovorum GM2 : Purification and Characterization

Abstract

CoASAc-independent phosphoenolpyruvate (PEP) carboxylase was purified from a serine-producing methylotroph, Hyphomi-crobium methylovorum GM2, and compared with those from other methylotrophs. The activity of thie enzyme was not affected by CoASAc, a well-known activator for enzymes from various hetero-trophs, NADH and ADP, effectors for PEP carboxylase from methylamine-grown Pseudomonas MA. This suggested that the H. methylovorum enzyme should be classified into the second group according to Utter and Kolenbrander (ref. 1) and different from that of Pseudomonas MA.