KEGG Orthology (KO) [BR:ko00001]
09100 Metabolism
09105 Amino acid metabolism
00360 Phenylalanine metabolism
K00500 phhA, PAH; phenylalanine-4-hydroxylase
00400 Phenylalanine, tyrosine and tryptophan biosynthesis
K00500 phhA, PAH; phenylalanine-4-hydroxylase
09108 Metabolism of cofactors and vitamins
00790 Folate biosynthesis
K00500 phhA, PAH; phenylalanine-4-hydroxylase
Enzymes [BR:ko01000]
1. Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.16 With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor
1.14.16.1 phenylalanine 4-monooxygenase
K00500 phhA, PAH; phenylalanine-4-hydroxylase
Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine hydroxylase and 4 alpha-carbinolamine dehydratase/DCoH as part of a three-component gene cluster.
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor
The active centre contains mononuclear iron(II). The reaction involves an arene oxide that rearranges to give the phenolic hydroxy group. This results in the hydrogen at C-4 migrating to C-3 and in part being retained. This process is known as the NIH-shift. The 4a-hydroxytetrahydropteridine formed can dehydrate to 6,7-dihydropteridine, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydropteridine must be enzymically reduced back to tetrahydropteridine, by EC 1.5.1.34, 6,7-dihydropteridine reductase, before it slowly rearranges into the more stable but inactive compound 7,8-dihydropteridine.
History
EC 1.14.16.1 created 1961 as EC 1.99.1.2, transferred 1965 to EC 1.14.3.1, transferred 1972 to EC 1.14.16.1, modified 2002, modified 2003, modified 2019
High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin.
