Literature summary for 2.7.11.14 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.

Search for more literature for 2.7.11.14

Cloned(Commentary)

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

Inhibitors

Inhibitors	Comment	Organism	Structure
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

Metals/Ions	Comment	Organism	Structure
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

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Purification (Commentary)

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

Source Tissue

Source Tissue	Comment	Organism	Textmining
retina	-	Bos taurus	-
retinal rod	-	Bos taurus	-

Subunits

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)