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Sequence of TY3H_RAT

EC Number:1.14.16.2

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
tyrosine 3-monooxygenase
P04177
Rattus norvegicus
498
55966
Reaction
L-tyrosine + a 5,6,7,8-tetrahydropteridine + O2 = L-dopa + a 4a-hydroxy-5,6,7,8-tetrahydropteridine
Other sequences found for EC No. 1.14.16.2

General information:

Sequence
show sequence in fasta format
  0 MPTPSAPSPQ PKGFRRAVSE QDAKQAEAVT SPRFIGRRQS LIEDARKERE AAAAAAAAAV
 60 ASSEPGNPLE AVVFEERDGN AVLNLLFSLR GTKPSSLSRA VKVFETFEAK IHHLETRPAQ
120 RPLAGSPHLE YFVRFEVPSG DLAALLSSVR RVSDDVRSAR EDKVPWFPRK VSELDKCHHL
180 VTKFDPDLDL DHPGFSDQVY RQRRKLIAEI AFQYKHGEPI PHVEYTAEEI ATWKEVYVTL
240 KGLYATHACR EHLEGFQLLE RYCGYREDSI PQLEDVSRFL KERTGFQLRP VAGLLSARDF
300 LASLAFRVFQ CTQYIRHASS PMHSPEPDCC HELLGHVPML ADRTFAQFSQ DIGLASLGAS
360 DEEIEKLSTV YWFTVEFGLC KQNGELKAYG AGLLSSYGEL LHSLSEEPEV RAFDPDTAAV
420 QPYQDQTYQP VYFVSESFND AKDKLRNYAS RIQRPFSVKF DPYTLAIDVL DSPHTIQRSL
480 EGVQDELHTL AHALSAIS
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1269004
Grima B.,Lamouroux A.,Blanot F.,Faucon Biguet N.,Mallet J.
Complete coding sequence of rat tyrosine hydroxylase mRNA.
Proc. Natl. Acad. Sci. U.S.A.
82
617-621
1985
1269007
Haycock J.W.,Haycock D.A.
Tyrosine hydroxylase in rat brain dopaminergic nerve terminals. Multiple-site phosphorylation in vivo and in synaptosomes.
J. Biol. Chem.
266
5650-5657
1991
1269008
Bevilaqua L.R.,Graham M.E.,Dunkley P.R.,von Nagy-Felsobuki E.I.,Dickson P.W.
Phosphorylation of Ser(19) alters the conformation of tyrosine hydroxylase to increase the rate of phosphorylation of Ser(40).
J. Biol. Chem.
276
40411-40416
2001
1269009
Goodwill K.E.,Sabatier C.,Marks C.,Raag R.,Fitzpatrick P.F.,Stevens R.C.
Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases.
Nat. Struct. Biol.
4
578-585
1997
1269010
Daubner S.C.,Melendez J.,Fitzpatrick P.F.
Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation.
Biochemistry
39
9652-9661
2000
1269011
Daubner S.C.,Moran G.R.,Fitzpatrick P.F.
Role of tryptophan hydroxylase phe313 in determining substrate specificity.
Biochem. Biophys. Res. Commun.
292
639-641
2002
1269012
Tsudzuki T.,Tsujita M.
Isoosmotic isolation of rat brain synaptic vesicles, some of which contain tyrosine hydroxylase.
J. Biochem.
136
239-243
2004
1269013
Nakashima A.,Mori K.,Kaneko Y.S.,Hayashi N.,Nagatsu T.,Ota A.
Phosphorylation of the N-terminal portion of tyrosine hydroxylase triggers proteasomal digestion of the enzyme.
Biochem. Biophys. Res. Commun.
407
343-347
2011
1269014
Goodwill K.E.,Sabatier C.,Stevens R.C.
Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 A resolution: self-hydroxylation of Phe300 and the pterin-binding site.
Biochemistry
37
13437-13445
1998
1269015
Zhang S.,Huang T.,Ilangovan U.,Hinck A.P.,Fitzpatrick P.F.
The solution structure of the regulatory domain of tyrosine hydroxylase.
J. Mol. Biol.
426
1483-1497
2014