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IUBMB Comments The enzyme has no activating compound but is specific for its substrate, with which it co-purifies. Requires Mg2+ EC 1.14.16.2 , tyrosine 3-monooxygenase, by phosphorylation.
Synonyms
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EC 2.7.1.124
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formerly
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kinase, tyrosine 3-monooxygenase (phosphorylating)
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ATP + [tyrosine-3-monooxygenase] = ADP + phospho-[tyrosine-3-monooxygenase]
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phospho group transfer
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ATP:[tyrosine-3-monoxygenase] phosphotransferase
The enzyme has no activating compound but is specific for its substrate, with which it co-purifies. Requires Mg2+. Activates EC 1.14.16.2, tyrosine 3-monooxygenase, by phosphorylation.
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ATP + [tyrosine 3-monooxygenase]
ADP + [tyrosine 3-monooxygenase] phosphate
ATP + [tyrosine 3-monooxygenase]
ADP + [tyrosine 3-monooxygenase] phosphate
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Substrates: -
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ATP + [tyrosine 3-monooxygenase]
ADP + [tyrosine 3-monooxygenase] phosphate
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Substrates: specific, incorporates 1 mol phosphate per mol enzyme tetramer
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ATP + [tyrosine 3-monooxygenase]
ADP + [tyrosine 3-monooxygenase] phosphate
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Substrates: phosphorylation site: Ser-40
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ATP + [tyrosine 3-monooxygenase]
ADP + [tyrosine 3-monooxygenase] phosphate
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Substrates: -
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additional information
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no requirement for Ca2+
additional information
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no requirement for Ca2+
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additional information
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no inhibition by EGTA
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additional information
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no requirement for cAMP
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additional information
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no requirement for cAMP
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from adrenal gland
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Highest Expressing Human Cell Lines
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partial, during purification the kinase remains associated with its substrate
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Pigeon, D.; Drissi-Daoudi, R.; Gros, F.; Thibault, J.
Copurification of tyrosine hydroxylase from rat pheochromocytoma, with a protein kinase activity
C. R. Acad. Sci. Paris Ser. 3
302
435-438
1986
Rattus norvegicus
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Pigeon, D.; Ferrara, P.; Gros, F.; Thibault, J.
Rat pheochromocytoma tyrosine hydroxylase is phosphorylated on serine 40 by an associated protein kinase
J. Biol. Chem.
262
6155-6158
1987
Rattus norvegicus
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