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Literature summary for 1.14.16.1 extracted from

  • Carluccio, C.; Fraternali, F.; Salvatore, F.; Fornili, A.; Zagari, A.
    Structural features of the regulatory ACT domain of phenylalanine hydroxylase (2013), PLoS ONE, 8, e79482.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
F39C the mutant enzyme shows reduced activity compared to the wild type Homo sapiens
F39L the mutant enzyme shows reduced activity compared to the wild type Homo sapiens
G46S the mutant enzyme shows reduced activity compared to the wild type Homo sapiens
I65S the mutant enzyme shows reduced activity compared to the wild type Homo sapiens
I65T the mutant enzyme shows reduced activity compared to the wild type Homo sapiens
I65V the mutant enzyme shows reduced activity compared to the wild type Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Iron contains iron Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
4 * 52000, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-phenylalanine + tetrahydrobiopterin + O2 Homo sapiens
-
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P00439
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + tetrahydrobiopterin + O2
-
Homo sapiens L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 52000, SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
PAH
-
Homo sapiens
phenylalanine hydroxylase
-
Homo sapiens