Information on EC 3.1.3.60 - phosphoenolpyruvate phosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.3.60
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RECOMMENDED NAME
GeneOntology No.
phosphoenolpyruvate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + H2O = pyruvate + phosphate
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
additional information
-
PEP phosphatase increases as active Fe decreases
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate phosphohydrolase
Also acts, but more slowly, on a wide range of other monophosphates.
CAS REGISTRY NUMBER
COMMENTARY hide
122319-89-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
two genotypes
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Manually annotated by BRENDA team
cv. Micro-Tom
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Manually annotated by BRENDA team
mung bean
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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seedlings of Citrus sinensis (L.) Osbeck cv. Xuegan are irrigated with Mg-deficient or Mg-sufficient nutrient solution every other day for 12 weeks. (PEPP) activity slightly increased in roots. In contrast, Mg-deficient leaves show decreased PEPP activity
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-naphthyl-phosphate + H2O
1-naphthol + phosphate
show the reaction diagram
-
-
-
-
?
2,3-diphosphoglycerate + H2O
?
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
glycerate + phosphate
show the reaction diagram
-
poor substrate
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
ADP + H2O
?
show the reaction diagram
ADP-glucose + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
ATP + H2O
?
show the reaction diagram
D-fructose 2,6-diphosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
D-gluconate 6-phosphate + H2O
D-gluconate + phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 1-phosphate + H2O
?
show the reaction diagram
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-
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?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
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poor substrate
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
GDP + H2O
?
show the reaction diagram
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poor substrate
-
-
?
IDP + H2O
?
show the reaction diagram
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poor substrate
-
-
?
O-phospho-L-threonine + H2O
L-threonine + phosphate
show the reaction diagram
-
-
-
-
?
O-phospho-L-tyrosine + H2O
L-tyrosine + phosphate
show the reaction diagram
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-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
phytic acid + H2O
?
show the reaction diagram
UDP + H2O
?
show the reaction diagram
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poor substrate
-
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?
additional information
?
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the enzyme seems to be required for fruit development
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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
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
additional information
?
-
-
the enzyme seems to be required for fruit development
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-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-phosphoglycerate
aspartate
-
competitive
ATP
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competitive
citrate
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competitive
CuSO4
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complete inhibition at 4 mM
D-fructose 1,6-bisphosphate
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complete inhibition at 5 mM, competitive
FeCl3
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complete inhibition at 4 mM
glutamate
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competitive
glyceraldhyde-3-phosphate
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competitive
Hg2+
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competitive towards Mg2+
iodoacetate
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Lead acetate
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70% inhibition at 8 mM
methylene blue
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after irradiation
MgADP
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41% inhibition at 0.5 mM, competitive
molybdate
N-ethylmaleimide
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-
Ni2+
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competitive towards Mg2+
oxalate
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competitive
p-chloromercuribenzoate
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reversible with excess of cysteine
phosphate
Rose bengal
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after irradiation
succinate
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competitive
ZnCl2
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complete inhibition at 4 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
2,3 diphosphoglycerate
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25°C, pH 5.6
1.21
3-phosphoglycerate
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25°C, pH 5.6
0.57 - 1.6
4-nitrophenyl phosphate
0.74 - 2.69
ADP
0.5 - 1.51
ATP
0.59
D-gluconate 6-phosphate
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25°C, pH 5.6
0.24
D-glucose 1-phosphate
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25°C, pH 5.6
1.47 - 2.01
D-glucose 6-phosphate
0.05 - 0.44
phosphoenolpyruvate
0.82 - 1.36
Phytic acid
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 3.3
3-phosphoglycerate
5
ATP
-
competitive, 30°C, pH 8.5
4.5
citrate
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competitive, 30°C, pH 8.5
0.22
Cu2+
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competitive towards Mg2+, 30°C, pH 8.5
0.06
D-fructose 1,6-bisphosphate
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25°C, pH 5.6
0.003
molybdate
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25°C, pH 5.6
3
oxalate
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competitive, 30°C, pH 8.5
0.085
phosphate
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25°C, pH 5.6
6.3
succinate
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competitive, 30°C, pH 8.5
0.023
Zn2+
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competitive towards Mg2+, 30°C, pH 8.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.05
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Vmax, purified enzyme, 30°C, pH 8.5
1.4
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purified enzyme, 30°C, pH 8.5
53
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purified enzyme, 25°C, pH 6.6
380
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purified enzyme, 25°C, pH 5.6
1225
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purified enzyme, 25°C, pH 5.6
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at pH 7.5 in Tris-HCl, or at pH 5.6 in sodium acetate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7.5
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6.5 - 10
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7.2 - 9.8
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half maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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the enzyme shows highly increased activity about 35 days after flowering
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
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SDS-PAGE, degradation product with 42000 Da
55000
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SDS-PAGE
56000
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gel filtration
57000
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SDS-PAGE
62000
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gel filtration
240000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 7.8
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stable
646426
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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4 min, 20% loss of activity
60
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4 min, 30% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, purified enzyme, 50 days, 50% loss of activity
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-15-4°C, 50 days, no loss of activity
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-80°C, purified enzyme, 6 months, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
copurifies with pyruvate kinase activity
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