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Literature summary for 2.7.11.6 extracted from

  • Pigeon, D.; Drissi-Daoudi, R.; Gros, F.; Thibault, J.
    Copurification of tyrosine hydroxylase from rat pheochromocytoma, with a protein kinase activity (1986), C. R. Acad. Sci. Paris Ser. 3, 302, 435-438.
    View publication on PubMed
Search for more literature for 2.7.11.6

Activating Compound

Activating Compound Comment Organism Structure
additional information no requirement for cAMP Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition by EGTA Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Rattus norvegicus
additional information no requirement for Ca2+ Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [tyrosine 3-monooxygenase] Rattus norvegicus
-
 ADP + [tyrosine 3-monooxygenase] phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial, during purification the kinase remains associated with its substrate Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
pheochromocytoma cell from adrenal gland Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [tyrosine 3-monooxygenase]
-
 Rattus norvegicus ADP + [tyrosine 3-monooxygenase] phosphate
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Rattus norvegicus