Reciprocal effects of an inhibitory factor on catalytic activity and noncatalytic cGMP binding sites of rod phosphodiesterase.

@article{Yamazaki1982ReciprocalEO,
  title={Reciprocal effects of an inhibitory factor on catalytic activity and noncatalytic cGMP binding sites of rod phosphodiesterase.},
  author={Akio Yamazaki and F Bartucca and Alan Ting and Mark W. Bitensky},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1982},
  volume={79 12},
  pages={3702-6}
}
In illuminated rod outer segment membranes, GTP and guanosine 5'-[beta, gamma-imido]triphosphate (p[NH]ppG) have reciprocal effects on cGMP phosphodiesterase (PDEase; 3':5'-cyclic-nucleotide 5'-nucleotidohydrolase, EC 3.1.4.17) activity and cGMP binding to noncatalytic sites on that enzyme. Two micromolar p[NH]ppG increased PDEase activity more than 2-fold while inhibiting cGMP binding more than 40%. Reduction of noncatalytic cGMP binding, which followed addition of p[NH]ppG, was not a result… CONTINUE READING