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Literature summary for 2.7.11.14 extracted from

  • Benovic, J.L.; Mayor, F.; Somers, R.L.; Caron, M.G.; Lefkowitz, R.J.
    Light-dependent phosphorylation of rhodopsin by beta-adrenergic receptor kinase (1986), Nature, 321, 869-872.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + rhodopsin Bos taurus
-
ADP + phosphorhodopsin
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
eye retina Bos taurus
-
retina rod cell outer segment Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.013
-
-
Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + beta-adrenergic receptor phosphorylates rhodopsin better than betaAR Bos taurus ADP + phospho-beta-adrenergic receptor
-
?
ATP + rhodopsin
-
Bos taurus ADP + phosphorhodopsin
-
?
ATP + rhodopsin light-dependent phosphorylation Bos taurus ADP + phosphorhodopsin
-
?
ATP + rhodopsin preferred substrate: photobleached rhodopsin Bos taurus ADP + phosphorhodopsin
-
?
ATP + rhodopsin phosphorylates serine and threonine residues in the carboxy-terminal region of opsin peptide Bos taurus ADP + phosphorhodopsin
-
?
additional information beta-adrenergic receptor kinase, EC 2.7.1.126, is also capable of rhodopsin phosphorylation in a light-dependent manner Bos taurus ?
-
?