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Information on EC 1.14.16.1 - phenylalanine 4-monooxygenase and Organism(s) Colwellia psychrerythraea and UniProt Accession Q47XN7

for references in articles please use BRENDA:EC1.14.16.1
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EC Tree
IUBMB Comments
The active centre contains mononuclear iron(II). The reaction involves an arene oxide that rearranges to give the phenolic hydroxy group. This results in the hydrogen at C-4 migrating to C-3 and in part being retained. This process is known as the NIH-shift. 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.
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This record set is specific for:
Colwellia psychrerythraea
UNIPROT: Q47XN7
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Word Map
The taxonomic range for the selected organisms is: Colwellia psychrerythraea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
phenylalanine hydroxylase, phenylalanine 4-monooxygenase, pheoh, phenylalanine 4-hydroxylase, phenylalanine monooxygenase, dicpah, cepah, l-phenylalanine 4-hydroxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phenylalanine hydroxylase
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oxygenase, phenylalanine 4-mono-
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PAH
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phenylalaninase
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phenylalanine 4-hydroxylase
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phenylalanine hydroxylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating)
The active centre contains mononuclear iron(II). The reaction involves an arene oxide that rearranges to give the phenolic hydroxy group. This results in the hydrogen at C-4 migrating to C-3 and in part being retained. This process is known as the NIH-shift. 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.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-73-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
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-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Flydal, M.I.; Martinez, A.
Phenylalanine hydroxylase: function, structure, and regulation
IUBMB Life
65
341-349
2013
Caenorhabditis elegans, Legionella pneumophila, Homo sapiens (P00439), Homo sapiens, Rattus norvegicus (P04176), Chromobacterium violaceum (P30967), Colwellia psychrerythraea (Q47XN7), Legionella pneumophila 130b
Manually annotated by BRENDA team