Literature summary extracted from

Andersen, O.A.; Stokka, A.J.; Flatmark, T.; Hough, E.
2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding (2003), J. Mol. Biol., 333, 747-757.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.14.16.1	in complex with 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin and substrate analogues 3-(2-thienyl)-L-alanine or L-norleucine	Homo sapiens

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.16.1	Homo sapiens	P00439	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
1.14.16.1	L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine	substrate binding triggers structural changes throughout the entire tetrameric enzyme	Homo sapiens	a

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.14.16.1	3-(2-thienyl)-L-alanine + tetrahydrobiopterin + O2	-	Homo sapiens	? + dihydrobiopterin + H2O	-	?
1.14.16.1	L-norleucine + tetrahydrobiopterin + O2	5% of the activity with 3-(2-thienyl)-L-alanine	Homo sapiens	? + dihydrobiopterin + H2O	-	?

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Release 2023.1 (January 2023)