KEGG   ENZYME: 1.14.16.7
Entry
EC 1.14.16.7                Enzyme                                 

Name
phenylalanine 3-monooxygenase;
PacX;
phenylalanine 3-hydroxylase
Class
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
Sysname
L-phenylalanine,tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating)
Reaction(IUBMB)
L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = 3-hydroxy-L-phenylalanine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine [RN:R12543]
Reaction(KEGG)
R12543;
(other) R10729
Substrate
L-phenylalanine [CPD:C00079];
5,6,7,8-tetrahydropteridine [CPD:C05650];
O2 [CPD:C00007]
Product
3-hydroxy-L-phenylalanine [CPD:C20807];
4a-hydroxy-5,6,7,8-tetrahydropteridine [CPD:C22239]
Comment
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, 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 1.14.16.7 created 2014, modified 2019
Orthology
K03393  phenylalanine 3-monooxygenase
Reference
1  [PMID:21615132]
  Authors
Zhang W, Ames BD, Walsh CT
  Title
Identification of phenylalanine 3-hydroxylase for meta-tyrosine biosynthesis.
  Journal
Biochemistry 50:5401-3 (2011)
DOI:10.1021/bi200733c
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.16.7
IUBMB Enzyme Nomenclature: 1.14.16.7
ExPASy - ENZYME nomenclature database: 1.14.16.7
BRENDA, the Enzyme Database: 1.14.16.7

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