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ENZYME

ENZYME entry: EC 1.14.16.7

PURL: https://purl.expasy.org/enzyme/EC/1.14.16.7
Accepted Name
phenylalanine 3-monooxygenase
Alternative Name(s)
phenylalanine 3-hydroxylase
Reaction catalysed
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = 3-hydroxy-L-phenylalanine + (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin
Comment(s)
  • The enzyme, characterized from the bacterium Streptomyces coeruleorubidus, forms 3-hydroxy-L-phenylalanine (i.e. m-L-tyrosine), which is one of the building blocks in the biosynthesis of the uridyl peptide antibiotics pacidamycins.
  • The 4a-hydroxytetrahydropteridine formed can dehydrate to 6,7- dihydropteridine, both spontaneously and by the action of EC 4.2.1.96.
  • The 6,7-dihydropteridine must be enzymically reduced back to tetrahydropteridine, by EC 1.5.1.34, before it slowly rearranges into the more stable but inactive compound 7,8-dihydropteridine.
Cross-references
Rhea expert-curated reactions1.14.16.7
ExplorEnz1.14.16.7
IUBMB Enzyme Nomenclature1.14.16.7
UniProtKB/Swiss-Prot
F5BFC8, PH3H_STRC4
BRENDA1.14.16.7
MetaCyc1.14.16.7
KEGG Ligand Database for Enzyme Nomenclature1.14.16.7
EC2PDB1.14.16.7
MEDLINEFind literature relating to 1.14.16.7

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