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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.14 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

EC Number Protein Variants Comment Organism
2.7.11.14 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
2.7.11.14 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
2.7.11.14 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
2.7.11.14 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
2.7.11.14 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
2.7.11.14 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
2.7.11.14 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
2.7.11.14 additional information a kinase mutant lacking the N-terminal recoverin binding site is unable to phosphorylate light-activated rhodopsin Bos taurus
2.7.11.14 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
2.7.11.14 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
2.7.11.14 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
2.7.11.14 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
2.7.11.14 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
2.7.11.14 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

EC Number Inhibitors Comment Organism Structure
2.7.11.14 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

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.14 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
2.7.11.14 Mg2+
-
Bos taurus

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.14 Bos taurus
-
-
-

Posttranslational Modification

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.14 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

EC Number Source Tissue Comment Organism Textmining
2.7.11.14 eye
-
Bos taurus
-
2.7.11.14 retina
-
Bos taurus
-

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.7.11.14 monomer
-
Bos taurus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.14 25
-
assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.14 7.4
-
assay at Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.14 ATP
-
Bos taurus