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ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
ADP + ?
CTP + D-fructose 1-phosphate
CDP + 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
TTP + D-fructose 1-phosphate
TDP + D-fructose 1,6-bisphosphate
UTP + D-fructose 1-phosphate
UDP + D-fructose 1,6-bisphosphate
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
-
-
-
-
?
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
-
-
-
-
?
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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ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
ADP + ?
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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4-chloromercuribenzoate
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
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
CTP
-
if concentration exceeds Mg2+ concentration
Cu2+
-
0.5 mM, 50% inhibition in the presence of 3 mM Mg2+
D-fructose 1,6-bisphosphate
D-fructose 6-phosphate
-
-
Hg2+
-
0.002 mM, 50% inhibition in the presence of 3 mM Mg2+
K+
-
300 mM, activates at 30 mM
NH4Cl
-
activation below 0.8 mM, inhibition above 0.8 M
Ni2+
-
3 mM, 50% inhibition in the presence of 3 mM Mg2+
phenylmethanesulfonyl fluoride
-
1 mM, 65% irreversible inhibition, 1.5 M ATP protect
UTP
-
if concentration exceeds Mg2+ concentration
ADP
-
competitive vs. ATP
ADP
-
2 mM, 45% inhibition, 5 mM ATP completely relieves inhibition
ATP
-
-
ATP
-
additional Mg2+ reverses; at a Mg2+/ATP ratio below 2
ATP
-
at a Mg2+/ATP ratio below 2; free form
ATP
-
at a Mg2+/ATP ratio below 2; free form
D-fructose 1,6-bisphosphate
-
noncompetitive vs. fructose 1-phosphate
D-fructose 1,6-bisphosphate
-
kinetics
D-fructose 1,6-bisphosphate
-
-
GTP
-
-
GTP
-
at a Mg2+/GTP ratio below 2
ITP
-
-
ITP
-
at a Mg2+/ITP ratio below 2
SO42-
-
-
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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Sapico, V.; Anderson, R.L.
D-fructose 1-phosphate kinase and D-fructose 6-phosphate kinase from Aerobacter aerogenes. A comparative study of regulatory properties
J. Biol. Chem.
244
6280-6288
1969
Klebsiella aerogenes
brenda
Baumann, L.; Baumann, P.
Catabolism of D-fructose and D-ribose by Pseudomonas doudoroffii. II. Properties of 1-phosphofructokinase and 6-phosphofructokinase
Arch. Microbiol.
105
241-248
1975
Oceanimonas doudoroffii
brenda
Hanson, T.E.; Anderson, R.L.
D-fructose 1-phosphate kinase, a new enzyme instrumental in the metabolism of D-fructose
J. Biol. Chem.
241
1644-1645
1966
Klebsiella aerogenes
brenda
Reeves, R.E.; Warren, L.G.; Hsu, D.S.
1-Phosphofructokinase from an anaerobe
J. Biol. Chem.
241
1257-1261
1966
[Clostridium] symbiosum
brenda
Anderson, R.L.; Hanson, T.E.; Sapico, V.
D-fructose-1-phosphate kinase
Methods Enzymol.
42C
63-66
1975
Klebsiella aerogenes
brenda
Van Hugo, H.; Gottschalk, G.
Purification and properties of 1-phosphofructokinase from Clostridium pasteurianum
Eur. J. Biochem.
48
455-463
1974
Clostridium pasteurianum
brenda
Du Toit, P.J.; Potgieter, D.J.J.; De Villiers, V.
Properties of 1-phosphofructokinase isolated from Clostridium pasteurianum
Enzymologia
43
285-300
1972
Clostridium pasteurianum
-
brenda
Buschmeier, B.; Hengstenberg, W.; Deutscher, J.
Purification and properties of 1-phosphofructokinase from Escherichia coli
FEMS Microbiol. Lett.
29
231-235
1985
Escherichia coli
-
brenda
Bang, S.S.; Baumann, P.; Sawyer, M.H.
Properties of 1-phosphofructokinase from Pseudomonas putida
Can. J. Microbiol.
23
721-725
1977
Pseudomonas putida
brenda
Veiga-da-Cunha, M.; Houyoux, A.; Van Schaftingen, E.
Overexpression and purification of fructose-1-phosphate kinase from Escherichia coli: Application to the assay of fructose 1-phosphate
Protein Expr. Purif.
19
48-52
2000
Escherichia coli
brenda
Hagopian, K.; Ramsey, J.J.; Weindruch, R.
Fructose metabolizing enzymes from mouse liver: influence of age and caloric restriction
Biochim. Biophys. Acta
1721
37-43
2005
Mus musculus
brenda
Barriere, C.; Veiga-da-Cunha, M.; Pons, N.; Guedon, E.; van Hijum, S.A.; Kok, J.; Kuipers, O.P.; Ehrlich, D.S.; Renault, P.
Fructose utilization in Lactococcus lactis as a model for low-GC gram-positive bacteria: its regulator, signal, and DNA-binding site
J. Bacteriol.
187
3752-3761
2005
Lactococcus lactis, Lactococcus lactis JIM8240
brenda
Su, Y.; Blake-Palmer, K.G.; Sorrell, S.; Javid, B.; Bowers, K.; Zhou, A.; Chang, S.H.; Qamar, S.; Karet, F.E.
Human H+ATPase a4 subunit mutations causing renal tubular acidosis reveal a role for interaction with phosphofructokinase-1
Am. J. Physiol. Renal Physiol.
295
F950-F958
2008
Homo sapiens
brenda
Martinez-Costa, O.H.; Sanchez-Martinez, C.; Sanchez, V.; Aragon, J.J.
Chimeric phosphofructokinases involving exchange of the N- and C-terminal halves of mammalian isozymes: implications for ligand binding sites
FEBS Lett.
581
3033-3038
2007
Homo sapiens
brenda
Peskov, K.; Goryanin, I.; Demin, O.
Kinetic model of phosphofructokinase-1 from Escherichia coli
J. Bioinform. Comput. Biol.
6
843-867
2008
Escherichia coli
brenda
Deng, H.; Yu, F.; Chen, J.; Zhao, Y.; Xiang, J.; Lin, A.
Phosphorylation of Bad at Thr-201 by JNK1 promotes glycolysis through activation of phosphofructokinase-1
J. Biol. Chem.
283
20754-20760
2008
Mus musculus
brenda
Russell, P.; Williams, A.; Marquez, K.; Tahir, Z.; Hosseinian, B.; Lam, K.
Some characteristics of rabbit muscle phosphofructokinase-1 inhibition by ascorbate
J. Enzyme Inhib. Med. Chem.
23
411-417
2008
Oryctolagus cuniculus
brenda
Pickl, A.; Johnsen, U.; Schoenheit, P.
Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase
J. Bacteriol.
194
3088-3097
2012
Haloferax volcanii (D4GYE6), Haloferax volcanii, Haloferax volcanii H1209 (D4GYE6)
brenda
Rangaswamy, V.; Altekar, W.
Characterization of 1-phosphofructokinase from halophilic archaebacterium Haloarcula vallismortis
Biochim. Biophys. Acta
1201
106-112
1994
Haloarcula vallismortis, Haloarcula vallismortis ATCC 34679
brenda
Funato, Y.; Hayashi, T.; Irino, Y.; Takenawa, T.; Miki, H.
Nucleoredoxin regulates glucose metabolism via phosphofructokinase 1
Biochem. Biophys. Res. Commun.
440
737-742
2013
Mus musculus
brenda
Chan, C.Y.; Parra, K.J.
Yeast phosphofructokinase-1 subunit Pfk2p is necessary for pH homeostasis and glucose-dependent vacuolar ATPase reassembly
J. Biol. Chem.
289
19448-19457
2014
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
brenda