Expasy logo

ENZYME

ENZYME entry: 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 <=> (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + 3-hydroxy-L-phenylalanine
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
BRENDA1.14.16.7
EC2PDB1.14.16.7
ExplorEnz1.14.16.7
PRIAM enzyme-specific profiles1.14.16.7
KEGG Ligand Database for Enzyme Nomenclature1.14.16.7
IUBMB Enzyme Nomenclature1.14.16.7
IntEnz1.14.16.7
MEDLINEFind literature relating to 1.14.16.7
MetaCyc1.14.16.7
Rhea expert-curated reactions1.14.16.7
UniProtKB/Swiss-Prot
F5BFC8, PH3H_STRC4

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot 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.-.-.-