Myxococcus xanthus M300 vegetative cells contained significant amounts of adenylate and guanylate cyclase activity. The latter was distributed between the 100000 g supernatant and pellet fractions, required divalent cations for activity and exhibited an apparent K of 1 mm. Adenylate cyclase activity was detected both in the l00000 g supernatant and pellet. The supernatant enzyme had an apparent K, of 220 PM with a Hill coefficient of 1.9, whereas the pellet enzyme had a K of 72 μM and a Hill coefficient of 1.0. The isoenzymes differed in their pH optima and divalent cation requirements for optimal activity. During development of Myxococcus xanthus, the nucleotide cyclase activities exhibited changes that were substantially consistent with the roles postulated for each in a previously proposed model.


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