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Literature summary for 2.7.11.14 extracted from

  • Higgins, M.K.; Oprian, D.D.; Schertler, G.F.
    Recoverin binds exclusively to an amphipathic peptide at the N terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase (2006), J. Biol. Chem., 281, 19426-19432.
    View publication on PubMed
Search for more literature for 2.7.11.14

Cloned(Commentary)

Cloned (Comment) Organism
expression of GST-tagged enzyme peptide fragments, expression of residues 1–562 of rhodopsin kinase in Spodoptera frugiperda Sf9 cells, expression of the truncation mutant comprising residues 32–562 in Escherichia coli as C-terminally His6-tagged protein Bos taurus

Protein Variants

Protein Variants Comment Organism
A11R site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
D2A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
E7A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
F15A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
F3A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
G4A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
L6A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
additional information a kinase mutant lacking the N-terminal recoverin binding site is unable to phosphorylate light-activated rhodopsin Bos taurus
N12A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
S13A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
S5A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
T8A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
V10A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus
V9A site-directed mutagenesis, the mutation of the residues leads to alterd binding of recoverin to the N-terminal fragment compared to the wild-type enzyme, kinetics constant, overview Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
recoverin binds exclusively to an amphipathic peptide at the N-terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase, calcium depletion causes release of recoverin from rhodopsin kinase, freeing the kinase to phosphorylate rhodopsin and to terminate the light response Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane Ca2+-bound enzyme Bos taurus 16020
-
soluble Ca2+-free enzyme Bos taurus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ induces a conformational change, while in the calciumfree form, the myristoyl group is held within a hydrophobic cleft, addition of calcium leads to its release and to membrane binding, inhibits rhodopsin binding to the enzyme via recoverin, which binds to the amphipathic peptide at the N-terminus of the enzyme and blocks rhodopsin binding Bos taurus
Mg2+
-
 Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + rhodopsin Bos taurus
-
 ADP + phosphorhodopsin
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein the enzyme is myristoylated in a Ca2+-dependent manner Bos taurus
phosphoprotein the enzyme performs autophosphorylation in a light-dependent manner Bos taurus

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged enzyme peptide fragments by glutathione affinity chromatography and gel filtration, recombinant His6-tagged truncation mutant 32–562 from Escherichia coli by nickel affinity chromatography and gel filtration, recombinant enzyme N-terminal fragment from Spodoptera frugiperda Sf9 cells by recoverin affinity chromatography and gel filtration to homogeneity Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
eye
-
 Bos taurus
-
retina
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + rhodopsin
-
 Bos taurus ADP + phosphorhodopsin
-
 ?
ATP + rhodopsin rhodopsin in rod outer segment membranes Bos taurus ADP + phosphorhodopsin
-
 ?
additional information the enzyme performs autophosphorylation in a light-dependent manner Bos taurus ?
-
 ?

Subunits

Subunits Comment Organism
monomer
-
 Bos taurus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Bos taurus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Bos taurus