Bovine rhodopsin: amino acid substitutions Asp-83----Asn and Glu-134----Gln prevent activation of cyclic GMP phosphodiesterase.
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.
Gurevich
V V
VV
Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR, Moscow, Region.
Zozulya
S A
SA
Zerf
E P
EP
Pokrovskaya
I D
ID
Obukhova
T A
TA
Garnovskaya
M N
MN
Dumler
I L
IL
Rychkova
M P
MP
D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D004247:DNA / Q000235:genetics; D004789:Enzyme Activation / Q000187:drug effects; D020558:GTP Phosphohydrolases / Q000378:metabolism; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D012243:Rhodopsin / Q000235:genetics* / Q000378:metabolism / Q000494:pharmacology
D004247:DNA; D012243:Rhodopsin; D015106:3',5'-Cyclic-GMP Phosphodiesterases; D020558:GTP Phosphohydrolases; C072504:transducin GTP phosphohydrolase