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Literature summary for 1.14.16.1 extracted from

  • Gunasekera, R.S.; Hyland, K.
    In vivo regulation of phenylalanine hydroxylase in the genetic mutant hph-1 mouse model (2009), Mol. Genet. Metab., 98, 264-272.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
5,6,7,8-tetrahydrobiopterin using L-phenylalanine as cosubstrate Mus musculus
0.04
-
L-phenylalanine using 5,6,7,8-tetrahydrobiopterin as cofactor Mus musculus
0.043
-
6-methyltetrahydropterin using L-phenylalanine as cosubstrate Mus musculus
0.25
-
L-phenylalanine using 6-methyltetrahydropterin as cofactor Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
-
Mus musculus L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
-
Mus musculus ?
-
?

Synonyms

Synonyms Comment Organism
PAH
-
Mus musculus
phenylalanine hydroxylase
-
Mus musculus

Cofactor

Cofactor Comment Organism Structure
5,6,7,8-tetrahydro-L-biopterin PAH can be activated up to 20times in the presence of its natural cofactor 5,6,7,8-tetrahydro-L-biopterin but cannot be activated in the presence of synthetic cofactors such as 6,7-dimethyltetrahydrobiopterin or 6-methyltetrahydropterin Mus musculus