Active sites of the cyclic GMP phosphodiesterase gamma-subunit of retinal rod outer segments

FEBS Lett. 1988 Jul 18;234(2):287-90. doi: 10.1016/0014-5793(88)80100-5.

Abstract

Monoclonal antibodies were prepared to the gamma-subunit of the cGMP phosphodiesterase. One of them gamma p-1, suppresses the activation of phosphodiesterase through the alpha-subunit of transducin. The gamma-subunit fragment 24-45 rich in Arg and Lys residues is involved in gamma p-1 binding and is essential for the gamma-subunit interaction with transducin. Carboxypeptidase Y cleaves off seven amino acid residues from the C-terminus of the gamma-subunit resulting in phosphodiesterase activation. Thus, the C-terminal fragment of gamma-subunit participates in phosphodiesterase inhibition.

MeSH terms

  • 3',5'-Cyclic-GMP Phosphodiesterases / immunology
  • 3',5'-Cyclic-GMP Phosphodiesterases / metabolism*
  • Animals
  • Antibodies, Monoclonal
  • Binding Sites
  • Cattle
  • Epitopes / analysis
  • Kinetics
  • Macromolecular Substances
  • Photoreceptor Cells / enzymology*
  • Rod Cell Outer Segment / enzymology*

Substances

  • Antibodies, Monoclonal
  • Epitopes
  • Macromolecular Substances
  • 3',5'-Cyclic-GMP Phosphodiesterases