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A role for pyridoxal phosphate in the control of dephosphorylation of phosphorylase a.

S. Yan,R. J. Uhing,R. F. Parrish,D. Metzler,D. Graves

Published 1979 in Journal of Biological Chemistry

ABSTRACT

The control of the dephosphorylation of phosphoryl- ase a by glucose or caffeine, but not by AMP requires the coenzyme, pyridoxal phosphate. The dephospho- rylation of apophosphorylase a and reconstituted phos- phorylase a derivatives prepared from analogs with less than two ionizable hydrogens at the 5’ position cannot be activated by glucose or caffeine. No dissociation of these inactive forms could be detected in the presence of glucose or caffeine in the ultracentrifuge, indicating that the coenzyme has an important effect on the binding, or structural changes, or both, induced by glucose or caffeine. The dephosphorylation of active phosphorylase a derivatives, pyridoxal-phosphorylase a in the presence of inorganic phosphite, or enzyme forms generated with 5’ side chains containing phos- phonate groups can be activated by glucose or caffeine. of phosphorylase a reconstituted with a-methylpyridoxal phosphate can be stimulated by caffeine but not by glucose. The phosphonate groups of the analogs have higher

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