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Literature summary extracted from

  • Ames, J.B.; Levay, K.; Wingard, J.N.; Lusin, J.D.; Slepak, V.Z.
    Structural basis for calcium-induced inhibition of rhodopsin kinase by recoverin (2006), J. Biol. Chem., 281, 37237-37245.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.14 expression of functional residues 1-25 of the enzyme as His-tagged peptide RK25 in Escherichia coli strain BL21(DE3) Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.14 recoverin calcium-induced inhibition, structural mechanism, recoverin serves as a calcium sensor that regulates rhodopsin kinase activity, binding structures, overview, NMR structure determination and analysis of the ternary complex RK25-Ca2+-recoverin Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.14 Ca2+ affects enzyme binding to rhodopsin, induces binding of recoverin to the enzyme inhibiting its activity, NMR structure determination and analysis of the ternary complex RK25-Ca2+-recoverin Bos taurus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.14 recombinant His-tagged enzyme fragment RK25 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Bos taurus

Source Tissue

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

Subunits

EC Number Subunits Comment Organism
2.7.11.14 More NMR structure determination and analysis of the ternary complex RK25-Ca2+-recoverin Bos taurus