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(Received for publication, March 6, 1996, and in revised form, April 23, 1996)
From the Department of Pharmacology, University of Texas
Southwestern Medical Center, Dallas, Texas 75235-9041
An engineered, soluble form of mammalian adenylyl
cyclase has been expressed in Escherichia coli and purified
by three chromatographic steps. The enzyme utilizes one molecule of ATP
to synthesize one molecule of cyclic AMP and pyrophosphate at a maximal
specific activity of 12.8 µmol/min/mg, corresponding to a turnover
number of 720 min
Volume 271, Number 28,
Issue of July 12, 1996
pp. 16967-16974
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
1. Although devoid of membrane spans,
the enzyme displays all of the regulatory properties that are common to
mammalian adenylyl cyclases. It is activated synergistically by
Gs
and forskolin and is inhibited by adenosine (P-site)
analogs with kinetic patterns that are identical to those displayed by
the native enzymes. The purified enzyme is also inhibited directly by
the G protein 
subunit complex. After adenovirus-mediated
expression in adenylyl cyclase-deficient HC-1 cells, the enzyme can be
stimulated synergistically by Gs-coupled receptors and
forskolin.
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