ENZYME entry: EC 220.127.116.11
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|(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 <=> (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine|
- 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
- The 6,7-dihydrobiopterin can be enzymically reduced back to
tetrahydrobiopterin, by EC 18.104.22.168, or slowly rearranges into the
more stable compound 7,8-dihydrobiopterin.
- Formerly EC 22.214.171.124 and EC 126.96.36.199.
|PRIAM enzyme-specific profiles||188.8.131.52|
|KEGG Ligand Database for Enzyme Nomenclature||184.108.40.206|
|IUBMB Enzyme Nomenclature||220.127.116.11|
|MEDLINE||Find literature relating to 18.104.22.168|
|Rhea expert-curated reactions||22.214.171.124|
|Q2KIH7, PH4H_BOVIN; ||P90925, PH4H_CAEEL; ||Q9A7V7, PH4H_CAUVC; |
|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; |
entries corresponding to 1.14.16.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-