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Literature summary extracted from

  • Palczewski, K.; Ohguro, H.; Premont, R.T.; Inglese, J.
    Rhodopsin kinase autophosphorylation. Characterization of site-specific mutations (1995), J. Biol. Chem., 270, 15294-15298.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.14 rhodopsin photolyzed rhodopsin stimulates Bos taurus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.14 expression of RK and mutants in COS-7 cells Bos taurus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.11.14 K491A mutant is unable to phosphorylate acidic peptides, residue participates in substrate binding Bos taurus
2.7.11.14 additional information mutations at the autophosphorylation region affect the Km for ATP and change the initial site of phosphorylation on photolyzed rhodopsin, influence of mutations on the affinity for heparin-Sepharose Bos taurus
2.7.11.14 S488A autophosphorylation site mutant with increased activity for the phosphorylation of rhodopsin in the dark Bos taurus
2.7.11.14 S488A S488A/T489A double mutant with almost eliminated autophosphorylation and increased ability to phosphorylate rhodopsin in the dark Bos taurus
2.7.11.14 S488A autophosphorylation site mutant with 50% reduced autophosphorylation Bos taurus
2.7.11.14 S488D autophosphorylation site mutant with 50% reduced autophosphorylation and increased ability to phosphorylate rhodopsin in the dark Bos taurus
2.7.11.14 S488D S488D/T489D double mutant with almost eliminated autophosphorylation Bos taurus
2.7.11.14 T489A S488A/T489A double mutant with almost eliminated autophosphorylation and increased ability to phosphorylate rhodopsin in the dark Bos taurus
2.7.11.14 T489A autophosphorylation site mutant with 50% reduced autophosphorylation Bos taurus
2.7.11.14 T489D autophosphorylation site mutant with 50% reduced autophosphorylation Bos taurus
2.7.11.14 T489D S488D/T489D double mutant with almost eliminated autophosphorylation Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.14 heparin modest inhibition Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.11.14 0.002 0.004 rhodopsin pH 7.5, 30°C, wild-type RK and mutants Bos taurus
2.7.11.14 0.005
-
 ATP pH 7.5, 30°C, S488D mutant Bos taurus
2.7.11.14 0.007
-
 ATP pH 7.5, 30°C, wild-type RK Bos taurus
2.7.11.14 0.012 0.015 ATP pH 7.5, 30°C, K491A or T489A mutant Bos taurus
2.7.11.14 0.025
-
 ATP pH 7.5, 30°C, S488D/T489D double mutant Bos taurus
2.7.11.14 0.14
-
 ATP pH 7.5, 30°C, S488A/T489A double mutant Bos taurus
2.7.11.14 0.166
-
 ATP pH 7.5, 30°C, S488A mutant Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.11.14 membrane membrane-bound Bos taurus 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
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 RK partially terminates the biochemical events that follow photon absorption 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 phosphoprotein major autophosphorylation sites: Ser-488, Thr-489, the autophosphorylation region of RK is involved in binding of ATP to the catalytic site, it may regulate selectivity of the site of phosphorylation and may influence the rate of RK dissociation from phosphorylated photolyzed rhodopsin, mechanism of RK regulation by autophosphorylation Bos taurus

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.14 native RK, recombinant RK and mutants expressed in COS-7 cells Bos taurus

Storage Stability

EC Number Storage Stability Organism
2.7.11.14 on ice, RK mutants, 2 days, stable Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.14 ATP + peptide acidic peptides, stimulated by photolyzed rhodopsin, K-491 of RK participates in substrate binding Bos taurus ADP + phosphopeptide
-
 ?
2.7.11.14 ATP + rhodopsin the autophosphorylation region of RK is involved in binding of ATP to the catalytic site and may regulate selectivity of the site of phosphorylation Bos taurus ADP + phosphorhodopsin
-
 ?
2.7.11.14 ATP + rhodopsin highly specific for photobleached rhodopsin Bos taurus ADP + phosphorhodopsin
-
 ?
2.7.11.14 ATP + rhodopsin phosphorylation sites of photolyzed rhodopsin Bos taurus ADP + phosphorhodopsin
-
 ?
2.7.11.14 ATP + rhodopsin domain structure Bos taurus ADP + phosphorhodopsin
-
 ?
2.7.11.14 ATP + rhodopsin RK partially terminates the biochemical events that follow photon absorption Bos taurus ADP + phosphorhodopsin
-
 ?
2.7.11.14 additional information not: apoprotein opsin Bos taurus ?
-
 ?
2.7.11.14 additional information not: unbleached rhodopsin Bos taurus ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.14 30
-
 assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.14 7.5
-
 assay at Bos taurus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.11.14 0.3
-
 heparin pH 7.5, 30°C Bos taurus