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Literature summary for 2.7.11.14 extracted from

  • Kelleher, D.J.; Johnson, G.L.
    Characterization of rhodopsin kinase purified from bovine rod outer segments (1990), J. Biol. Chem., 265, 2632-2639.
    View publication on PubMed
Search for more literature for 2.7.11.14

Inhibitors

Inhibitors Comment Organism Structure
Synthetic peptide corresponding to sequences within opsin loops 3-4 and 5-6 and the C-terminus, bleached rhodopsin as substrate Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic study of autophosphorylation, Km values for synthetic peptide substrates: 5 mM or greater, pH 7.4 Bos taurus
0.00062
-
 rhodopsin pH 7.4, fully phosphorylated enzyme Bos taurus
0.00064
-
 rhodopsin pH 7.4, minimally phosphorylated enzyme Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane rod membranes Bos taurus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
62000
-
 1 * 62000, SDS-PAGE Bos taurus
62000
-
 1 * 62000, unphosphorylated kinase, SDS-PAGE Bos taurus
64000
-
 1 * 64000, autophosphorylated kinase, SDS-PAGE Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + rhodopsin Bos taurus major regulatory mechanism for the control of photorhodopsin transduction pathway ADP + phosphorhodopsin
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein autophosphorylation of serine residues, uneffected by the presence of bleached rhodopsin, results in a transition of the molecular mass to 64 kDa, not a major regulatory mechanism for control of kinase activity Bos taurus
phosphoprotein enzyme is autophosphorylated in the absence of rhodopsin Bos taurus

Purification (Commentary)

Purification (Comment) Organism
-
 Bos taurus

Reaction

Reaction Comment Organism Reaction ID
ATP + rhodopsin = ADP + phosphorhodopsin mechanism Bos taurus
a

Source Tissue

Source Tissue Comment Organism Textmining
eye retina Bos taurus
-
eye dark-adapted Bos taurus
-
retina rod cell outer segment Bos taurus
-
retina from dark-adapted eyes Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.01
-
 pH 7.4 Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + peptide corresponding to the C-terminus and loop 5-6 of opsin, poor substrates, phosphorylates serine and threonine residues in each peptide Bos taurus ADP + phosphopeptide
-
 ?
ATP + rhodopsin catalyzes multisite phosphorylation of purified rhodopsin in phospholipid vesicles Bos taurus ADP + phosphorhodopsin
-
 ?
ATP + rhodopsin light-dependent phosphorylation Bos taurus ADP + phosphorhodopsin
-
 ?
ATP + rhodopsin phosphorylates bovine rhodopsin Bos taurus ADP + phosphorhodopsin
-
 ?
ATP + rhodopsin highly specific for photobleached rhodopsin Bos taurus ADP + phosphorhodopsin
-
 ?
ATP + rhodopsin major regulatory mechanism for the control of photorhodopsin transduction pathway Bos taurus ADP + phosphorhodopsin
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 62000, SDS-PAGE Bos taurus
monomer 1 * 62000, unphosphorylated kinase, SDS-PAGE Bos taurus
monomer 1 * 64000, autophosphorylated kinase, SDS-PAGE Bos taurus

pH Optimum

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