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Literature summary for 2.7.11.14 extracted from

  • Shichi, H.; Somers, R.L.
    Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin kinase (1978), J. Biol. Chem., 253, 7040-7046.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
spermidine slight stimulation Bos taurus

General Stability

General Stability Organism
monovalent cations, e.g. K+ or NH4+, and 15% glycerol stabilize to some extent Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
5'-AMP 1 mM, 50% inhibition Bos taurus
adenosine 1 mM, 50% inhibition Bos taurus
Digitonin 0.1%, 50% inhibition Bos taurus
emulphogene 0.1%, 50% inhibition Bos taurus
additional information not inhibited by cAMP; not inhibited by cGMP; not inhibited by K+ Bos taurus
Na+ 0.1 M, 90% inhibition Bos taurus
Zn2+ 1 mM, 90% inhibition Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.008
-
ATP pH 7.4, 37°C Bos taurus
0.4
-
GTP pH 7.4, 37°C Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound Bos taurus 16020
-
membrane membrane-bound Lithobates pipiens 16020
-
membrane phosphorylation occurs preferentially in newly formed discs Bos taurus 16020
-
membrane phosphorylation occurs preferentially in newly formed discs Lithobates pipiens 16020
-
membrane rod membranes Bos taurus 16020
-
membrane rod membranes Lithobates pipiens 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Bos taurus
Mg2+ requirement Lithobates pipiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
1 * 50000, SDS-PAGE Bos taurus
53000
-
gel filtration Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + rhodopsin Bos taurus enzyme in vivo is probably inactive in the dark, but is almost fully activated in the light ADP + phosphorhodopsin
-
?
ATP + rhodopsin Lithobates pipiens enzyme in vivo is probably inactive in the dark, but is almost fully activated in the light ADP + phosphorhodopsin
-
?

Organic Solvent Stability

Organic Solvent Comment Organism
urea 5 M, almost complete denaturation of enzyme Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Lithobates pipiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
87-110fold Bos taurus

Source Tissue

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.026 0.033
-
Bos taurus

Storage Stability

Storage Stability Organism
3°C, 0.1 M KCl, 1 week, 50% loss of activity Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + rhodopsin phosphorylates rhodopsin in the disc-membrane Bos taurus ADP + phosphorhodopsin
-
ir
ATP + rhodopsin phosphorylates rhodopsin in the disc-membrane Lithobates pipiens ADP + phosphorhodopsin
-
ir
ATP + rhodopsin highly specific for rhodopsin Bos taurus ADP + phosphorhodopsin
-
ir
ATP + rhodopsin highly specific for rhodopsin Lithobates pipiens ADP + phosphorhodopsin
-
ir
ATP + rhodopsin light-dependent phosphorylation Bos taurus ADP + phosphorhodopsin
-
ir
ATP + rhodopsin preferred substrate: ATP Bos taurus ADP + phosphorhodopsin
-
ir
ATP + rhodopsin phosphorylates bovine rhodopsin Bos taurus ADP + phosphorhodopsin
-
ir
ATP + rhodopsin rhodopsin with multiphosphorylation sites Bos taurus ADP + phosphorhodopsin
-
ir
ATP + rhodopsin enzyme in vivo is probably inactive in the dark, but is almost fully activated in the light Bos taurus ADP + phosphorhodopsin
-
?
ATP + rhodopsin enzyme in vivo is probably inactive in the dark, but is almost fully activated in the light Lithobates pipiens ADP + phosphorhodopsin
-
?
GTP + rhodopsin can replace ATP to a lesser extent Bos taurus GDP + phosphorhodopsin
-
?
additional information not: protamine Bos taurus ?
-
?
additional information not: casein, phosvitin, histones Bos taurus ?
-
?
additional information not: casein, phosvitin, histones Lithobates pipiens ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 50000, SDS-PAGE Bos taurus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Bos taurus
37
-
assay at Lithobates pipiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information ATP: 2.2 mol of phosphate bound/min, GTP: 0.12 mol of phosphate bound/min Bos taurus

pH Optimum

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