ENZYME entry: EC 1.14.16.1

Accepted Name
Phenylalanine 4-monooxygenase.
Alternative Name(s)
PAH.
Phenylalaninase.
Phenylalanine 4-hydroxylase.
Phenylalanine hydroxylase.
Reaction catalysed
L-phenylalanine + tetrahydrobiopterin + O(2) <=> L-tyrosine + 4a-hydroxytetrahydrobiopterin
Cofactor(s)
Iron.
Comment(s)
  • The reaction involves an arene oxide which rearranges to give the phenolic hydroxy group.
  • This results in the hydrogen at C-4 migrating to C-3 and in part being retained, a process known as the NIH-shift.
  • The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7- dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96.
  • The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34, or slowly rearranges into the more stable compound 7,8-dihydrobiopterin.
  • Formerly EC 1.14.3.1 and EC 1.99.1.2.
Cross-references
PROSITEPDOC00316
BRENDA1.14.16.1
EC2PDB1.14.16.1
ExplorEnz1.14.16.1
PRIAM enzyme-specific profiles1.14.16.1
KEGG Ligand Database for Enzyme Nomenclature1.14.16.1
IUBMB Enzyme Nomenclature1.14.16.1
IntEnz1.14.16.1
MEDLINEFind literature relating to 1.14.16.1
MetaCyc1.14.16.1
UniProtKB/Swiss-Prot
Q2KIH7, PH4H_BOVIN;  P90925, PH4H_CAEEL;  Q9A7V7, PH4H_CAUCR;  
P30967, PH4H_CHRVO;  Q54XS1, PH4H_DICDI;  P17276, PH4H_DROME;  
P00439, PH4H_HUMAN;  P16331, PH4H_MOUSE;  P43334, PH4H_PSEAE;  
Q8XU39, PH4H_RALSO;  P04176, PH4H_RAT;  Q98D72, PH4H_RHILO;  
Q9KLB8, PH4H_VIBCH;  

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