Literature summary for 1.14.16.1 extracted from

Chadha, N.; Tiwari, A.K.; Kumar, V.; Milton, M.D.; Mishra, A.K.
In silico thermodynamics stability change analysis involved in BH4 responsive mutations in phenylalanine hydroxylase QM/MM and MD simulations analysis (2015), J. Biomol. Struct. Dyn., 33, 573-583 .

Search for more literature for 1.14.16.1

Protein Variants

Protein Variants	Comment	Organism
A313T	the mutation leads to thermodynamic stability change upon folding	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	contains non-heme iron	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	-	-

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
tetrahydrobiopterin	-	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)