Information on EC 1.14.16.7 - phenylalanine 3-monooxygenase

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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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-hydroxytetra-6-methyltetrahydrobiopterin
show the reaction diagram
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-
?
L-phenylalanine + tetrahydrobiopterin + O2
3-hydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
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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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
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
addition of ferrous ammonium sulfate increases the product yield more than 3-fold
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
increases the product yield more than 72%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
6-methyltetrahydropterin
pH 6.2, 22C
1.1
L-phenylalanine
pH 6.2, 22C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021
6-methyltetrahydropterin
Streptomyces coeruleorubidus
F5BFC8
pH 6.2, 22C
0.022
L-phenylalanine
Streptomyces coeruleorubidus
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C187F
hydroxylation rate is reduced to less than 4% compared to the rate of wild-type enzyme
C187F/T202G
hydroxylation rate is comparable to that of wild-type enzyme. Less than 8% of m-Tyr compared to p-Tyr is formed
T202G
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