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Literature summary for 2.7.11.14 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
Search for more literature for 2.7.11.14

Activating Compound

Activating Compound Comment Organism Structure
rhodopsin photolyzed rhodopsin stimulates Bos taurus

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
K491A mutant is unable to phosphorylate acidic peptides, residue participates in substrate binding Bos taurus
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
S488A autophosphorylation site mutant with increased activity for the phosphorylation of rhodopsin in the dark Bos taurus
S488A S488A/T489A double mutant with almost eliminated autophosphorylation and increased ability to phosphorylate rhodopsin in the dark Bos taurus
S488A autophosphorylation site mutant with 50% reduced autophosphorylation Bos taurus
S488D autophosphorylation site mutant with 50% reduced autophosphorylation and increased ability to phosphorylate rhodopsin in the dark Bos taurus
S488D S488D/T489D double mutant with almost eliminated autophosphorylation Bos taurus
T489A S488A/T489A double mutant with almost eliminated autophosphorylation and increased ability to phosphorylate rhodopsin in the dark Bos taurus
T489A autophosphorylation site mutant with 50% reduced autophosphorylation Bos taurus
T489D autophosphorylation site mutant with 50% reduced autophosphorylation Bos taurus
T489D S488D/T489D double mutant with almost eliminated autophosphorylation Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
heparin modest inhibition Bos taurus

KM Value [mM]

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + rhodopsin Bos taurus RK partially terminates the biochemical events that follow photon absorption ADP + phosphorhodopsin
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Storage Stability

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

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

pH Optimum

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

Ki Value [mM]

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