Bovine rhodopsin: amino acid substitutions Asp-83----Asn and Glu-134----Gln prevent activation of cyclic GMP phosphodiesterase

V V Gurevich; S A Zozulya; E P Zerf; I D Pokrovskaya; T A Obukhova; M N Garnovskaya; I L Dumler; M P Rychkova

Bovine rhodopsin: amino acid substitutions Asp-83----Asn and Glu-134----Gln prevent activation of cyclic GMP phosphodiesterase

Biomed Sci. 1990;1(5):527-30.

Authors

V V Gurevich¹, S A Zozulya, E P Zerf, I D Pokrovskaya, T A Obukhova, M N Garnovskaya, I L Dumler, M P Rychkova

Affiliation

¹ Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR, Moscow, Region.

PMID: 1966786

Abstract

Two bovine rhodopsin mutants with substitutions of negatively charged residues within transmembrane domains II and III by uncharged ones (Asp-83----Asn and Glu-134----Gln) were constructed. Both mutants stimulated transducin GTPase with slightly lowered efficiency, but were completely unable to activate cyclic GMP phosphodiesterase.

MeSH terms

3',5'-Cyclic-GMP Phosphodiesterases / metabolism
Amino Acid Sequence
Animals
Base Sequence
Cattle
DNA / genetics
Enzyme Activation / drug effects
GTP Phosphohydrolases / metabolism
In Vitro Techniques
Molecular Sequence Data
Mutagenesis, Site-Directed
Rhodopsin / genetics*
Rhodopsin / metabolism
Rhodopsin / pharmacology

Substances

DNA
Rhodopsin
3',5'-Cyclic-GMP Phosphodiesterases
GTP Phosphohydrolases
transducin GTP phosphohydrolase