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Literature summary for 1.14.16.2 extracted from

  • Chow, M.S.; Eser, B.E.; Wilson, S.A.; Hodgson, K.O.; Hedman, B.; Fitzpatrick, P.F.; Solomon, E.I.
    Spectroscopy and kinetics of wild-type and mutant tyrosine hydroxylase: mechanistic insight into O2 activation (2009), J. Am. Chem. Soc., 131, 7685-7698.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
E332A the E332A mutant hydroxylates less than 1% L-tyrosine compared to wild type and does not produce 4a-hydroxytetrahydrobiopterin Rattus norvegicus
S395A the S395A mutant produces 4a-hydroxytetrahydrobiopterin at the same rate as wild type, but does so in predominantly uncoupled reaction (2% of wild type enzyme L-tyrosine hydroxylation) Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required for activity Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tyrosine + 5,6,7,8-tetrahydrobiopterin + O2
-
Rattus norvegicus 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin
-
?
L-tyrosine + DL-6-methyl-5,6,7,8-tetrahydropterin + O2
-
Rattus norvegicus ?
-
?

Synonyms

Synonyms Comment Organism
tyrosine hydroxylase
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
tetrahydrobiopterin
-
Rattus norvegicus