By G. Alan Robison

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Whether adenyl cyclase is in fact composed of distinct subunits is of course unknown. The enzyme has been obtained in a soluble form from several bacterial species (Hirata and Hayaishi, 1967; Brana, 1969; Tao and Lipmann, 1969), but its chemical constitution has not been studied. These bacterial enzymes do not respond to mammalian hormones, but adenyl cyclase from Brevibacterium liquifaciens is stimulated by pyruvate and several other α-keto acids (Hirata and Hayaishi, 1967). It is tempting to suppose that the mechanism by which pyruvate stimulates this enzyme is basically similar to that by which hormones act in mammalian systems, but whether this is valid or not remains to be seen.

In cells in which two or more structurally different hormones are known to be capable of stimulating adenyl cyclase, the question arises as to whether all of the hormones stimulate the same enzyme, or whether there are separate enzymes for each hormone. The available evidence suggests that in rat adipocytes all of the hormones stimulate the same enzyme, since the effects of maximally effective concentrations of hormones are not additive (Butcher et al, 1968; Birnbaumer et al, 1969). Instead, the activity of adenyl cyclase in the presence of two hormones only reaches the activity produced by the more effective of the two.

Attention can also be called to an interesting paper by Lefkowitz et al. (1970). These investigators used high pressure disintegration iri the presence of phosphatidylethanolamine to obtain a "solubilized" preparation of adenyl cyclase from an adrenal tumor. This preparation could be fractionated with the retention of sensitivity to stimulation by ACTH. The relation between ACTH-binding and the stimulation of adenyl cyclase activity was very striking in these experiments, emphasizing further the close relation that exists between hormone receptors and adenyl cyclase.

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