Information on EC 1.14.16.7 - phenylalanine 3-monooxygenase

for references in articles please use BRENDA:EC1.14.16.7
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The expected taxonomic range for this enzyme is: Streptomyces coeruleorubidus

EC NUMBER
COMMENTARY hide
1.14.16.7
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RECOMMENDED NAME
GeneOntology No.
phenylalanine 3-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine + tetrahydrobiopterin + O2 = 3-hydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine,tetrahydrobiopterin:oxygen oxidoreductase (3-hydroxylating)
The enzyme 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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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F5BFC8
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
F5BFC8
the enzyme forms 3-hydroxy-L-phenylalanine (i.e. m-L-tyrosine) which is one of the building blocks in the biosynthesis of pacidamycins
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 + 6-methyltetrahydropterin + O2
3-hydroxy-L-phenylalanine + 4a-hydroxy-6-methyltetrahydropterin
show the reaction diagram
F5BFC8
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
3-hydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
F5BFC8
the enzyme forms 3-hydroxy-L-phenylalanine (i.e. m-L-tyrosine) which is one of the building blocks in the biosynthesis of pacidamycins
3-hydroxy-L-phenylalanine i.e. m-L-Tyr
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?
additional information
?
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F5BFC8
no activity with D-Phe, L-Tyr, and L-Trp
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
3-hydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
F5BFC8
the enzyme forms 3-hydroxy-L-phenylalanine (i.e. m-L-tyrosine) which is one of the building blocks in the biosynthesis of pacidamycins
3-hydroxy-L-phenylalanine i.e. m-L-Tyr
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
F5BFC8
addition of ferrous ammonium sulfate increases the product yield more than 3-fold
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
F5BFC8
increases the product yield more than 72%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
6-methyltetrahydropterin
F5BFC8
pH 6.2, 22C
1.1
L-phenylalanine
F5BFC8
pH 6.2, 22C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021
6-methyltetrahydropterin
F5BFC8
pH 6.2, 22C
0.022
L-phenylalanine
F5BFC8
pH 6.2, 22C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned as an N-terminal six-His-tagged protein, expressed in Escherichia coli, wild-type and mutant enzymes C187F, T202G and C187F/T202G
F5BFC8
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C187F
F5BFC8
hydroxylation rate is reduced to less than 4% compared to the rate of wild-type enzyme
C187F/T202G
F5BFC8
hydroxylation rate is comparable to that of wild-type enzyme. Less than 8% of m-Tyr compared to p-Tyr is formed
T202G
F5BFC8
hydroxylation rate is comparable to that of wild-type enzyme. The ratio of product p-Tyr to m-Tyr is changed to 2:1 for the T202G mutant, which represents a 60-fold increase in the preference for p-Tyr over m-Tyr formation