Information on EC 1.14.99.20 - phylloquinone monooxygenase (2,3-epoxidizing)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.99.20
-
RECOMMENDED NAME
GeneOntology No.
phylloquinone monooxygenase (2,3-epoxidizing)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phylloquinone + AH2 + O2 = 2,3-epoxyphylloquinone + A + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
phylloquinone,hydrogen-donor:oxygen oxidoreductase (2,3-epoxidizing)
-
CAS REGISTRY NUMBER
COMMENTARY hide
54596-37-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fetus, neonate, 1-18 years
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron + H2O
show the reaction diagram
phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron donor + H2O
show the reaction diagram
additional information
?
-
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
phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-chloro-3-phytyl-1,4-naphthoquinone
-
-
glutathione peroxidase
-
competitive inhibitor
-
Tetrachloro-4-pyridinol
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutamate-containing substrates
-
bound to the vitamin K-dependent carboxylase converts its vitamin K epoxidase function from an inactive to an active state
-
Mn2+
-
activating effect is limited to peptide substrate with vicinal glutamyl residues
propeptide
-
bound to the vitamin K-dependent carboxylase converts its vitamin K epoxidase function from an inactive to an active state
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00667
Phe-Leu-Glu-Glu-Leu
Bos taurus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00077 - 0.00088
-
-
0.00466
-
-
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17
-
enzyme assay
25
-
enzyme assay
37
-
enzyme assay
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
preincubation for 15 min at 37C results in an almost complete inhibition of the epoxidation
-
stable for several days when left on ice, freezing and thawing destroys the activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, lyophilized, stable for up to 1 month
-
-80C, 20% glycerol
-
-80C, soluble enzyme preparation, at least 5% glycerol, stable to multiple freeze and thaw cycles
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in chinese hamster ovary cells CHO-Dukx-B11
-
wild-type and mutants of bovine enzyme species expressed in baculovirus-infected Spodoptera frugiperda cells
-
wild-type and mutants of bovine enzyme species expressed in chinese hamster ovary cells CHO-Dukx-B11
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H160A
-
94% of wild-type activity
H287A
-
163% of wild-type activity
H381A
-
142% of wild-type activity
K218A
-
no residual activity, but exogenous amines restore activity and its degree depends on the basicity of the amine