Abstract
Phosphorylase kinase and calcium-free calmodulin are digested by human immunodeficiency virus-1 protease. In phosphorylase kinase, the α subunit is preferentially hydrolyzed at arg 748-val 749. The β subunit is cleaved only slowly at leu 678-pro 679, and calmodulin, the integral δ subunit of phosphorylase kinase, is not cleaved at all. However, free calmodulin in the calcium-depleted form showed to be a good substrate for the protease. Here the cleavage occurs at phe 65-pro 66 and met 71-met 72. This fast hydrolysis of free calmodulin can be blocked by micromolar concentrations of Ca 2+ or millimolar concentrations of Mg 2+.
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