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InterPro: IPR005962 Tyrosine 3-monooxygenase

Protein matchesHelp
UniProtKB
Matches:
44 proteins
AccessionHelp IPR005962 Tyr_3_mOase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR019773 Tyrosine 3-monooxygenase-like
Contains IPR018301 Aromatic amino acid hydroxylase, iron/copper binding site
IPR019774 Aromatic amino acid hydroxylase, C-terminal
GO Term annotationHelp
Process GO:0042423 catecholamine biosynthetic process
GO:0055114 oxidation reduction
Function GO:0004511 tyrosine 3-monooxygenase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Tyrosine 3-monooxygenase (EC:1.14.16.2), is a member of the family of tetrameric, biopterin-dependent aromatic amino acid hydroxylases found in metazoans. It is closely related to tetrameric phenylalanine-4-hydroxylase and tryptophan 5-monooxygenase, and more distantly related to the monomeric phenylalanine-4-hydroxylase found in some Gram-negative bacteria. It catalyses the first step in catecholamine biosynthesis.

L-tyrosine + tetrahydropteridine + O2 = 3,4-dihydroxy-L-phenylalanine + dihydropteridine + H2O.

Structural linksHelp
SCOP: d.178.1.1
CATH: 1.10.800.10
Database linksHelp
Enzyme: EC:1.14.16.2
PRIAM: PRI003744

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR005962 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O17446 Tyrosine 3-monooxygenase

P04177 Tyrosine 3-monooxygenase

P07101 Tyrosine 3-monooxygenase

P18459 Tyrosine 3-monooxygenase

P24529 Tyrosine 3-monooxygenase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR019773 Tyrosine 3-monooxygenase-like
IPR019774 Aromatic amino acid hydroxylase, C-terminal
IPR005962 Tyrosine 3-monooxygenase
IPR001273 Aromatic amino acid hydroxylase
IPR018301 Aromatic amino acid hydroxylase, iron/copper binding site
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp

Additional ReadingHelp
Goodwill KE, Sabatier C, Marks C, Raag R, Fitzpatrick PF, Stevens RC.
Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases.
Nat. Struct. Biol. 4 1997 578-85 [PubMed: 9228951]
http://dx.doi.org/10.1038/nsb0797-578
Goodwill KE, Sabatier C, Stevens RC.
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 1998 13437-45 [PubMed: 9753429]
http://dx.doi.org/10.1021/bi981462g
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InterPro 24.0