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A catalytic fragment, 71-290/ derived from limited chymotryptic digestion of phosphorylase b kinase (Harris, W. R. et al., [1990] J. Biol. Chem., 265, 11740-11745), is reported to have about six-fold greater specific activity than does the 7 subunit-calmodulin complex. To test whether there is an inhibitory domain located outside the catalytic core of the y subunit, full-length wild-type and seven truncated forms of 7 were expressed in E. coli. Recombinant proteins accumulate in the inclusion bodies and can be isolated, solubilized, renatured, and purified further by ammonium sulfate precipitation and Q-Sepharose column. Four out of seven truncated mutants show similar (71.353 and 7i.34i) or less (71-331 and 71.275) specific activity than does the full-length wild-type 7, 71.386Three truncated forms, 71.316, 71.300/ and 71.290 have molar specific activities approximately twice as great as those of the full-length wild-type 7 and the nonactivated holoenzyme. All recombinant 7s exhibit similar values for both substrates, i.e., about 18 /zM for phosphorylase b and about 75 /zM for MgATP. Three truncated 7 s , 7 1 . 3 1 6 / 7 i-3oo/ and 7 1 . 2 9 0 / have a 1.9to 2.5-fold greater catalytic efficiency (%nax/^) than that of the full-length wild-type 7 and a 3.5to 4.5-fold greater efficiency than that of the

Expression, purification, characterization, and site-directed mutagenesis of phosphorylase kinase [upsilon] subunit