Information on EC 2.7.1.56 - 1-phosphofructokinase

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

EC NUMBER
COMMENTARY hide
2.7.1.56
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RECOMMENDED NAME
GeneOntology No.
1-phosphofructokinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + D-fructose 1-phosphate = ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
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fructose degradation
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degradation of hexoses
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-fructose-phosphate 6-phosphotransferase
ITP, GTP or UTP can replace ATP.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-03-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain JIM8240
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Manually annotated by BRENDA team
strain JIM8240
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Manually annotated by BRENDA team
wild-type strain 75
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
ATP + D-fructose 6-phosphate
ADP + ?
show the reaction diagram
CTP + D-fructose 1-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
GTP + D-fructose 1-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
ITP + D-fructose 1-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
TTP + D-fructose 1-phosphate
TDP + D-fructose 1,6-bisphosphate
show the reaction diagram
UTP + D-fructose 1-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
additional information
?
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important role for PFK-1 in normal proton pump function. Loss of a-subunit/PFK-1 interaction is likely to decrease the stability of the metabolon formed by various H+ATPase subunits (notably E and a) and glycolytic components (aldolase and PFK-1)
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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
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
ATP + D-fructose 6-phosphate
ADP + ?
show the reaction diagram
additional information
?
-
-
important role for PFK-1 in normal proton pump function. Loss of a-subunit/PFK-1 interaction is likely to decrease the stability of the metabolon formed by various H+ATPase subunits (notably E and a) and glycolytic components (aldolase and PFK-1)
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CsCl
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stimulates
Fe2+
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3 mM, 50% of activity with Mn2+
KCl
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stimulates, optimal concentration: 1.2 M
Na+
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30-50 mM, 1.5fold activation
NaCl
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50% of the stimulation compared to KCl
NH4Cl
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activation below 0.8 mM, inhibition above 0.8 M
RbCl
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stimulates
Zn2+
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3 mM, 34% of activity with Mn2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
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5,5'-dithiobis(2-nitrobenzoic acid)
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ascorbate
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inhibition is dependent on concentration of PFK-1. No inhibition above 200 nM PFK-1. It is concluded that ascorbate inhibits PFK-1 dimer (and perhaps monomers) but not PFK-1 tetramers
CTP
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if concentration exceeds Mg2+ concentration
Cu2+
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0.5 mM, 50% inhibition in the presence of 3 mM Mg2+
D-fructose 1,6-bisphosphate
D-fructose 6-phosphate
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Hg2+
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0.002 mM, 50% inhibition in the presence of 3 mM Mg2+
K+
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300 mM, activates at 30 mM
MgATP2-
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NH4Cl
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activation below 0.8 mM, inhibition above 0.8 M
Ni2+
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3 mM, 50% inhibition in the presence of 3 mM Mg2+
phenylmethanesulfonyl fluoride
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1 mM, 65% irreversible inhibition, 1.5 M ATP protect
SO42-
UTP
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if concentration exceeds Mg2+ concentration
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
reduced glutathione
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serves as the best sulphydryl compound for optimum activity. Cysteine, 2-mercaptoethanol and dithiothreitol can substitute for glutathione contributing about 80% of the activity
additional information
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no activation by pyruvate, phosphoenolpyruvate, AMP, cAMP, citrate, fructose 6-phosphate, glucose 6-phosphate, 6-phosphogluconate or 2-keto-3-deoxy-6-phosphogluconate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 1.44
ATP
0.13 - 0.8
D-Fructose 1-phosphate
1.12
D-fructose 6-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42C
0.36
fructose 1-phosphate
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pH 7.1, 30C, in the absence of KCl
0.67
ITP
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pH 8.0, 25C
additional information
additional information
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Km-values of chimeric enzymes
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1200
D-Fructose 1-phosphate
Haloferax volcanii
D4GYE6
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42C
671
34
D-fructose 6-phosphate
Haloferax volcanii
D4GYE6
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42C
87
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28 - 0.68
ADP
6.1
D-fructose-1,6-bisphosphate
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pH 7.6, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.27
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activity in crude extracts
6.9 - 81.6
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additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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50 mM Tris-HCl
8 - 8.8
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50% activity at pH 7.1
8.5
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50 mM NH4HCO3
10.7
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steady increase in activity from pH 7.5 to 10.7. Activity at pHs above 10.7 are not tested due to limitations of the assay system
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10.2
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very low activity at pH 5.5, approx. half-maximal activity at pH 6.3 and pH 10.2
7 - 9.8
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approx. half-maximal activity at pH 7 and 9.8
7 - 8.7
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approx. 80% of maximal activity at pH 7. approx. half-maximal activity at pH 8.7
7 - 8
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44% of maximal activity at pH 7 and 81% of maximal activity at pH 8
7.5 - 10.7
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steady increase in activity from pH 7.5 to 10.7. Activity at pHs above 10.7 are not tested due to limitations of the assay system
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21400
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1 * 21400 + 1 * 35500, SDS-PAGE, after treatment with 8 M urea and 2-mercaptoethanol
28500
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1 * 28500 + 1 * 40000, SDS-PAGE, after treatment with 2-mercaptoethanol
30000
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2 * 30000, SDS-PAGE
34000
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2 * 34000, recombinant enzyme, SDS-PAGE
35500
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1 * 21400 + 1 * 35500, SDS-PAGE, after treatment with 8 M urea and 2-mercaptoethanol
38000
2 * 38000, SDS-PAGE
40000
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1 * 28500 + 1 * 40000, SDS-PAGE, after treatment with 2-mercaptoethanol
57000
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gel filtration
62500
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low-speed sedimentation equilibrium
63100
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gel filtration
63200
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sucrose density gradient centrifugation
70000
gel filtration
75000
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gel filtration
76000
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gel filtration, sucrose density gradient ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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pH 9.0, 0.1 M KCl, 50 mM Tris-HCl, 80% loss of activity after 2 h. The enzyme is fully active for more than 2 months in 2.5 M KCl/50 mM Tris-HCl buffer, pH 9.0. Phosphate at 50 mM concentration stabilizes the enzyme against inactivation in 0.1 M KCI for about 24 h. (NH4)2SO4 though inhibitory for expression of the enzyme activity is stabilizing
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against water, 0.9% NaCl or buffer, stable to
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freeze-thawing, stable to
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partially purified enzyme withstands freeze-thawing, purified enzyme loses 50% of activity by freezing and thawing
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Tris-HCl buffer in purification and electrophoresis leads to partial denaturation and loss of activity, stable in phosphate buffer
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, 3 days, 70% loss of activity
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-20C, 100 mM (NH4)2SO4, pH 7.5, at least 8 months
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-20C, 100 mM (NH4)2SO4, pH 7.5, several months, no loss of activity
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-20C, 50 mM phosphate buffer, pH 7.5, 1 year, no loss of activity
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-20C, crude enzyme extract prepared in water, at least 3 weeks
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-80C, 20% glycerol, 2 years, no loss of activity
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4C, 0.8-1.3 mg protein/ml in 50 mM phosphate buffer, pH 7, 0.5 mM dithiothreitol, 5-10% loss of activity
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4C, 1 week, about 30% loss of activity
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4C, a few days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-Sephadex, partially purified
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ammonium sulfate, Sephadex G25, DEAE-Sepharose
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chimeric enzyme
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CM-Sephadex, calcium phosphate gel, Sephadex G-100, DEAE-Sephadex, hydroxyapatite
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DEAE-cellulose, ammonium sulfate, hydroxylapatite, Sephadex G-75, DEAE-cellulose
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Ni-NTA column chromatography and Superdex 200 gel filtration
partial
protamine sulfate, ammonium sulfate, heat, Sephadex G-100, DEAE-cellulose, partially purified
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
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wild-type and chimeric enzymes are expressed in a PFK-deficient Saccharomyces cerevisiae strain
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is specifically upregulated in fructose-grown cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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construction of two chimeric phosphofructokinases in which the N- and C-terminal halves of human muscle and ascites tumor cells are exchanged
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