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Information on EC 2.7.1.56 - 1-phosphofructokinase
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2.7.1.56 1-phosphofructokinaseIUBMB Comments
ITP, GTP or UTP can replace ATP.
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Word Map
- 2.7.1.56
-
fructose-specific
-
fructose-grown
-
entner-doudoroff
- hpr
-
phosphoenolpyruvate-dependent
- 1,6-bisphosphate
-
embden-meyerhof
-
phosphoenolpyruvate:fructose
-
iifru
-
embden-meyerhof-parnas
- ribokinase
- capsulata
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
1-phosphofructokinase, fructose-1-phosphate kinase, 1-pfk, fructose 1-phosphate kinase, d-fructose-1-phosphate kinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-PFK
1PFK
D-fructose-1-phosphate kinase
-
-
-
-
FruC
fructose 1-phosphate kinase
-
-
-
-
fructose-1-phosphate kinase
kinase, 1-phosphofructo- (phosphorylating)
-
-
-
-
PFK-1
PFK1
PFK2
pfkB
phosphofructokinase 1
-
-
-
-
phosphofructokinase-1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + D-fructose 1-phosphate = ADP + D-fructose 1,6-bisphosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-fructose-phosphate 6-phosphotransferase
ITP, GTP or UTP can replace ATP.
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CAS REGISTRY NUMBER
COMMENTARY
37278-03-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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)
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with D-fructose 6-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with D-glucose 6-phosphate, D-glucose 1-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with D-fructose 6-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with D-fructose 6-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with D-fructose 6-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with D-glucose 6-phosphate, D-glucose 1-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with D-glucose 6-phosphate, D-glucose 1-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
specific for D-fructose 1-phosphate, no activity with L-fructose 1-phosphate, D-fructose, D-mannose 6-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
specific for D-fructose 1-phosphate, no activity with L-fructose 1-phosphate, D-fructose, D-mannose 6-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with sorbose 1-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
inducible enzyme
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
involved in D-fructose metabolism
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
key enzyme of glucose metabolism
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
phosphorylation of Bad by JNK1 is required for glycolysis through activation of phosphofructokinase-1, one of the key enzymes that catalyze glycolysis
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with D-fructose 6-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
sole pathway of D-fructose metabolism in several Pseudomonas species
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with D-fructose 6-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
no activity with sorbose 1-phosphate
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
inducible enzyme
-
?
ATP + D-fructose 6-phosphate
ADP + ?
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
-
-
?
ATP + D-fructose 6-phosphate
ADP + ?
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
-
-
?
CTP + D-fructose 1-phosphate
CDP + D-fructose 1,6-bisphosphate
-
10% of activity with ATP
-
?
CTP + D-fructose 1-phosphate
CDP + D-fructose 1,6-bisphosphate
-
besides ATP, pyridine nucleotides such as CTP and TTP are equally effective phosphoryl donors. GTP and UTP can contribute only 60% of the activity
-
-
?
CTP + D-fructose 1-phosphate
CDP + D-fructose 1,6-bisphosphate
-
besides ATP, pyridine nucleotides such as CTP and TTP are equally effective phosphoryl donors. GTP and UTP can contribute only 60% of the activity
-
-
?
CTP + D-fructose 1-phosphate
CDP + D-fructose 1,6-bisphosphate
-
poor substrate
-
?
GTP + D-fructose 1-phosphate
GDP + D-fructose 1,6-bisphosphate
-
60% of activity with ATP
-
?
GTP + D-fructose 1-phosphate
GDP + D-fructose 1,6-bisphosphate
-
besides ATP, pyridine nucleotides such as CTP and TTP are equally effective phosphoryl donors. GTP and UTP can contribute only 60% of the activity
-
-
?
GTP + D-fructose 1-phosphate
GDP + D-fructose 1,6-bisphosphate
-
besides ATP, pyridine nucleotides such as CTP and TTP are equally effective phosphoryl donors. GTP and UTP can contribute only 60% of the activity
-
-
?
GTP + D-fructose 1-phosphate
GDP + D-fructose 1,6-bisphosphate
-
35% of activity with ATP
-
?
GTP + D-fructose 1-phosphate
GDP + D-fructose 1,6-bisphosphate
-
69% of activity with ATP
-
?
GTP + D-fructose 1-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
GTP + D-fructose 1-phosphate
GDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 1-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ITP + D-fructose 1-phosphate
IDP + D-fructose 1,6-bisphosphate
-
43% of activity with ATP
-
?
ITP + D-fructose 1-phosphate
IDP + D-fructose 1,6-bisphosphate
-
45% of activity with ATP
-
?
ITP + D-fructose 1-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
ITP + D-fructose 1-phosphate
IDP + D-fructose 1,6-bisphosphate
-
-
-
?
TTP + D-fructose 1-phosphate
TDP + D-fructose 1,6-bisphosphate
-
besides ATP, pyridine nucleotides such as CTP and TTP are equally effective phosphoryl donors. GTP and UTP can contribute only 60% of the activity
-
-
?
TTP + D-fructose 1-phosphate
TDP + D-fructose 1,6-bisphosphate
-
besides ATP, pyridine nucleotides such as CTP and TTP are equally effective phosphoryl donors. GTP and UTP can contribute only 60% of the activity
-
-
?
TTP + D-fructose 1-phosphate
TDP + D-fructose 1,6-bisphosphate
-
poor substrate
-
?
UTP + D-fructose 1-phosphate
UDP + D-fructose 1,6-bisphosphate
-
20% of activity with ATP
-
?
UTP + D-fructose 1-phosphate
UDP + D-fructose 1,6-bisphosphate
-
besides ATP, pyridine nucleotides such as CTP and TTP are equally effective phosphoryl donors. GTP and UTP can contribute only 60% of the activity
-
-
?
UTP + D-fructose 1-phosphate
UDP + D-fructose 1,6-bisphosphate
-
besides ATP, pyridine nucleotides such as CTP and TTP are equally effective phosphoryl donors. GTP and UTP can contribute only 60% of the activity
-
-
?
UTP + D-fructose 1-phosphate
UDP + D-fructose 1,6-bisphosphate
-
poor substrate
-
?
UTP + D-fructose 1-phosphate
UDP + D-fructose 1,6-bisphosphate
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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)
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
inducible enzyme
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
involved in D-fructose metabolism
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
key enzyme of glucose metabolism
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
phosphorylation of Bad by JNK1 is required for glycolysis through activation of phosphofructokinase-1, one of the key enzymes that catalyze glycolysis
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
sole pathway of D-fructose metabolism in several Pseudomonas species
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
-
inducible enzyme
-
?
ATP + D-fructose 6-phosphate
ADP + ?
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
-
-
?
ATP + D-fructose 6-phosphate
ADP + ?
physiological substrate, the enzyme exhibits a36fold higher catalytic efficiency towards D-fructose 1-phosphate compared to D-fructose 6-phosphate
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
K+
Mg2+
Mn2+
NH4+
additional information
Mg2+
-
is the most active divalent cation and can not be replaced either by Mn2+ or any other divalent cation. The optimal ratio of ATP/Mg2+ is 1:1
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
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
phenylmethanesulfonyl fluoride
-
1 mM, 65% irreversible inhibition, 1.5 M ATP protect
D-fructose 1,6-bisphosphate
-
noncompetitive vs. fructose 1-phosphate
additional information
-
not inhibited by cAMP, pyruvate, phosphoenolpyruvate; not inhibited by citrate; not inhibited by D-fructose 6-phosphate; not inhibited by D-glucose 1-phosphate; not inhibited by D-glucose 6-phosphate; not inhibited by monovalent cations, glucose, ADPglucose, UDPglucose, NAD(H), NADP(H), dihydroxyacetone phosphate, glyceraldehyde 3-phosphate, 3-phosphoglycerate, CoA, acetyl-CoA, acetoacetyl-CoA; not inhibited by phosphate, AMP
-
additional information
-
not inhibited by D-fructose 6-phosphate; not inhibited by D-glucose 1-phosphate; not inhibited by D-glucose 6-phosphate
-
additional information
-
not inhibited by ATP; not inhibited by D-glucose 1-phosphate; not inhibited by D-glucose 6-phosphate; not inhibited by nucleoside monophosphates or diphosphates, D-mannose 6-phosphate, D-fructose, L-fructose 1-phosphate; not inhibited by phosphate, AMP
-
additional information
-
not inhibited by cAMP, pyruvate, phosphoenolpyruvate; not inhibited by citrate; not inhibited by CTP and UTP; not inhibited by D-fructose 6-phosphate; not inhibited by L-glutamate; not inhibited by phosphate, AMP
-
additional information
-
not inhibited by 6-phosphogluconate, 2-oxo-3-deoxy-6-phosphogluconate; not inhibited by cAMP, pyruvate, phosphoenolpyruvate; not inhibited by citrate; not inhibited by CTP and UTP; not inhibited by D-fructose 6-phosphate; not inhibited by D-glucose 6-phosphate; not inhibited by phosphate, AMP
-
additional information
-
not inhibited by D-fructose 6-phosphate; not inhibited by sorbose 1-phosphate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
reduced glutathione
-
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
-
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
LITERATURE
IMAGE
1.12
D-fructose 6-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
0.08
ATP
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
0.31
D-Fructose 1-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1200
D-Fructose 1-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
34
D-fructose 6-phosphate
in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.7
-
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
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10.2
-
very low activity at pH 5.5, approx. half-maximal activity at pH 6.3 and pH 10.2
7 - 8
-
44% of maximal activity at pH 7 and 81% of maximal activity at pH 8
7 - 8.7
-
approx. 80% of maximal activity at pH 7. approx. half-maximal activity at pH 8.7
7.5 - 10.7
-
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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