Information on EC 2.7.1.11 - 6-phosphofructokinase

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

EC NUMBER
COMMENTARY
2.7.1.11
-
RECOMMENDED NAME
GeneOntology No.
6-phosphofructokinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
mechanism
-
ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
mechanism
-
ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
probably a random or compulsory-order ternary complex mechanism at pH 8.0
-
ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
iso-ordered bi-bi mechanism
-
ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
K-type allosteric enzyme, ordered sequential mechanism at pH 6.4
-
ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
allosteric regulated enzyme, ping-pong bi-bi mechanism or according to Sumi and Ui, allosteric ping-pong II mechanism
-
ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
structure-oriented allosteric four-state model describing substrate and effector actions on PFK
-
ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
sequential random mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
1,3-propanediol biosynthesis (engineered)
-
Biosynthesis of antibiotics
-
Biosynthesis of secondary metabolites
-
formaldehyde assimilation II (RuMP Cycle)
-
Fructose and mannose metabolism
-
Galactose metabolism
-
glycolysis
BRENDA
BRENDA
BRENDA
Glycolysis / Gluconeogenesis
-
glycolysis I (from glucose 6-phosphate)
-
glycolysis II (from fructose 6-phosphate)
-
glycolysis III (from glucose)
-
glycolysis IV (plant cytosol)
-
glycolysis VI (metazoan)
-
Metabolic pathways
-
Methane metabolism
-
Microbial metabolism in diverse environments
-
Pentose phosphate pathway
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-fructose-6-phosphate 1-phosphotransferase
D-Tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. UTP, CTP and ITP can act as donors. Not identical with EC 2.7.1.105 6-phosphofructo-2-kinase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1-phosphofructokinase
-
-
6-phosphofructo 1-kinase
-
-
6-phosphofructo-1-kinase
-
-
6-phosphofructo-1-kinase
-
-
6-phosphofructo-1-kinase
-
-
6-phosphofructo-1-kinase
-
-
6-phosphofructokinase, platelet type
-
-
-
-
6-phosphofructose 1-kinase
-
-
-
-
6-phosphofructose-1-kinase
-
-
-
-
APE0012
Q9YG89
gene name
APE0012
Aeropyrum pernix DSM 11879
Q9YG89
gene name
-
At2g22480
Q8VYN6
-
At4g26270
Q94AA4
-
At4g29220
Q9M0F9
-
At4g32840
Q9M076
-
At5g56630
Q9C5J7
-
At5g61580
Q9FKG3
-
ATP-dependent 6-phosphofructokinase
-
-
ATP-dependent 6-phosphofructokinase
-
-
ATP-dependent PFK
-
-
ATP-dependent phosphofructokinase
-
-
-
-
ATP-dependent phosphofructokinase
A1XM06, A1XM07
-
ATP-PFK
-
-
-
-
ATP-PFK
Q9YG89
-
ATP-PFK
Aeropyrum pernix DSM 11879
Q9YG89
-
-
ATP: D-fructose-6-phosphate-1-phosphotransferase
-
-
ATP: D-fructose-6-phosphate-1-phosphotransferase
-
-
ATP:D-fructose-6-phosphate-1-phosphotransferase
-
-
D-fructose-6-phosphate 1-phosphotransferase
-
-
-
-
fructose 6-phosphate kinase
-
-
-
-
fructose 6-phosphokinase
-
-
-
-
hosphofructokinase-1
-
-
kinase, phosphofructo- (phosphorylating)
-
-
-
-
muscle-type phosphofructokinase
-
PFKM
nucleotide triphosphate-dependent phosphofructokinase
-
-
-
-
PFK
-
-
-
-
PFK
Saccharomyces cerevisiae PS1
P16862
-
-
PFK
-
-
PFK-1
-
-
PFK-1
-
-
Pfk-2
P06999
isoform
PFK-L
-
-
PFK-M
-
-
PFK1
-
-
-
-
PFK2
-
-
-
-
PFKM
-
-
PFKMS
-
spermatogenic cell-specific PFKM variant isozyme
phospho-1,6-fructokinase
-
-
-
-
phosphofructo-1-kinase
-
-
phosphofructokinase
-
-
-
-
phosphofructokinase
-
-
phosphofructokinase
P00512
-
phosphofructokinase
-
-
phosphofructokinase
-
-
phosphofructokinase
-
-
-
phosphofructokinase 1
-
-
-
-
phosphofructokinase 1
P00511
-
phosphofructokinase 1
P16862
-
phosphofructokinase 1
Saccharomyces cerevisiae PS1
P16862
-
-
phosphofructokinase M
-
-
phosphofructokinase-1
-
-
phosphofructokinase-1
-
-
phosphofructokinase-1
-
-
phosphofructokinase-1
-
-
phosphofructokinase-2
-
-
phosphofructokinase-2
P06999
isoform
phosphofructokinase-M
-
-
phosphohexokinase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-80-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
hyperthermophilic crenarchaeote
UniProt
Manually annotated by BRENDA team
Aeropyrum pernix DSM 11879
-
UniProt
Manually annotated by BRENDA team
methylotrophic bacterium
SwissProt
Manually annotated by BRENDA team
honey bee, sp. carnica, collecting worker bees
-
-
Manually annotated by BRENDA team
female parasitic nematode, from small intestine of pig
-
-
Manually annotated by BRENDA team
strain B60
-
-
Manually annotated by BRENDA team
strains A158, TE22, and TE23
Uniprot
Manually annotated by BRENDA team
Aspergillus niger B60
strain B60
-
-
Manually annotated by BRENDA team
e.g. Bacillus cereus, Bacillus megaterium, Bacillus mycoides, Bacillus subtilis 168M
-
-
Manually annotated by BRENDA team
bumblebee
-
-
Manually annotated by BRENDA team
calf; ox
-
-
Manually annotated by BRENDA team
blowfly
-
-
Manually annotated by BRENDA team
green alga
-
-
Manually annotated by BRENDA team
Macf, cv. Marsh, grapefruit
-
-
Manually annotated by BRENDA team
2 isoenzymes
-
-
Manually annotated by BRENDA team
cucumber, cv. Fletcher
-
-
Manually annotated by BRENDA team
carrot
-
-
Manually annotated by BRENDA team
PFK mRNA, PFK protein levels and PFK activity slowly decrease during development
SwissProt
Manually annotated by BRENDA team
Dunaliella marina
green alga
-
-
Manually annotated by BRENDA team
strain H200
-
-
Manually annotated by BRENDA team
Entamoeba histolytica H200
strain H200
-
-
Manually annotated by BRENDA team
strains PRL-R3, wild-type, and its mutant DD31
-
-
Manually annotated by BRENDA team
K10 or K12 strains Hfr3000, DF1651, DF500, DF443, DF1651B1, AMIR20, PFK1 and PFK2
-
-
Manually annotated by BRENDA team
mutant strains R72H and I127A; strain DF1020, containing overproducing plasmid pHE1007; strain DF1020, containing overproducing plasmid TG-1
-
-
Manually annotated by BRENDA team
strain DF1020, containing overproducing plasmid pHE1007
-
-
Manually annotated by BRENDA team
strain DF1020, containing overproducing plasmid pHE1007; strain DF1020, containing overproducing plasmid pHE1012
-
-
Manually annotated by BRENDA team
Escherichia coli DF1020
strain DF1020, containing overproducing plasmid pHE1007
-
-
Manually annotated by BRENDA team
Escherichia coli DF1020
strain DF1020, containing overproducing plasmid pHE1007; strain DF1020, containing overproducing plasmid pHE1012
-
-
Manually annotated by BRENDA team
Escherichia coli DF1020
strain DF1020, containing overproducing plasmid pHE1007; strain DF1020, containing overproducing plasmid TG-1
-
-
Manually annotated by BRENDA team
liver fluke, from bile duct of infected cattle
-
-
Manually annotated by BRENDA team
expressed in PFK-deficient Escherichia coli DF1020 cells
-
-
Manually annotated by BRENDA team
jerboa, euthermic and hibernating
-
-
Manually annotated by BRENDA team
strain C10
-
-
Manually annotated by BRENDA team
Lactococcus lactis C10
strain C10
-
-
Manually annotated by BRENDA team
gypsy moth
-
-
Manually annotated by BRENDA team
green alga
-
-
Manually annotated by BRENDA team
C-type PFK
SwissProt
Manually annotated by BRENDA team
L. cv. Cavendish, banana, isoenzymes PFK I and PFK II
-
-
Manually annotated by BRENDA team
Oceanimonas doudoroffii M1
strain M1
-
-
Manually annotated by BRENDA team
rainbow trout
-
-
Manually annotated by BRENDA team
european flounder
-
-
Manually annotated by BRENDA team
adult male Wistar
-
-
Manually annotated by BRENDA team
castor bean, cv. Baker 296, dwarf, hybrid, plastid and cytosolic isoenzymes
-
-
Manually annotated by BRENDA team
active dried yeast
-
-
Manually annotated by BRENDA team
baker's yeast, preferred source: pitching yeast
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae PS1
-
UniProt
Manually annotated by BRENDA team
strain CBS1057, PFK-1
-
-
Manually annotated by BRENDA team
Schizosaccharomyces pombe CBS1057
strain CBS1057, PFK-1
-
-
Manually annotated by BRENDA team
wild potato species
-
-
Manually annotated by BRENDA team
tomato, var. Eurocross BB
-
-
Manually annotated by BRENDA team
potato, cv. Record, Hertha or Cara, isoforms I-IV
-
-
Manually annotated by BRENDA team
gilthead sea bream
-
-
Manually annotated by BRENDA team
A3(2), strain M145
SwissProt
Manually annotated by BRENDA team
pfkA3 gene; A3(2), strain M145
SwissProt
Manually annotated by BRENDA team
; boar
-
-
Manually annotated by BRENDA team
protozoan, phenoset A
-
-
Manually annotated by BRENDA team
freshwater turtle
-
-
Manually annotated by BRENDA team
Schizotrypanum
-
-
Manually annotated by BRENDA team
i.e. Vigna mungo, black gram
-
-
Manually annotated by BRENDA team
maize
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
phosphofructo-1-kinase deficiency leads to a severe cardiac and hematological disorder in addition to skeletal muscle glycogenosis, the lack of PFK activity blocks glycolysis and results in considerable glycogen storage and low ATP content, although erythrocytes of PFK knockout mice preserve 50% of PFK activity, they show strong reduction of 2,3-biphosphoglycerate concentrations and hemolysis, PFK knockout mice exhibit high lethality and skeletal muscle glycogenosis
malfunction
-
mutations in the muscle 6-phosphofructokinase gene cause Tarui disease
physiological function
-
Pfk activity is required for the full in vivo fitness of Salmonella enterica serovar Typhimurium with functional redundancy between genes pfkA and pfkB
physiological function
-
isozyme PFKA is required for growth on glucose as sole carbon source. The isoform is also required for survival of hypoxic non-replicating Mycobaterium tuberculosis but is not required for virulence and survival in the mouse model of tuberculosis infection
physiological function
-
the enzyme catalyzes the first committed and rate-determining step of glycolysis and thus represents an essential metabolic control point or node for carbohydrate utilization
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
-
isozyme PFKA is required for growth on glucose as sole carbon source. The isoform is also required for survival of hypoxic non-replicating Mycobaterium tuberculosis but is not required for virulence and survival in the mouse model of tuberculosis infection
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,N6-etheno-ATP + D-fructose 6-phosphate
1,N6-etheno-ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
1-carboxymethyl-ATP + D-fructose 6-phosphate
1-carboxymethyl-ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
90% of activity with with ATP
-
?
2-amino-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
2-amino-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
6-mercapto-9-beta-D-ribofuranosylpurine 5'-triphosphate + D-fructose 6-phosphate
6-mercapto-9-beta-D-ribofuranosylpurine 5'-diphosphate + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + adenosine
ADP + ?
show the reaction diagram
-, Q9YG89
-
-
-
?
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-, key enzyme of glucose metabolism
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
-
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
-
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
P78985
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
A1XM06, A1XM07, -
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
-
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Dunaliella marina
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
-
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
P90521
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Q9WUA3
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-, Q8VU09
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-, Q9YG89
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-, Q9YG89
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Q9YG89
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
O08333, Q9FC99, Q9L1L8, -
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
P00512
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
P06999
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
P00511
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
P16862
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
fructose 6-phosphate shows negative cooperativity at low concentrations and positive cooperativity at high concentrations
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
35fold lower reverse reaction velocity
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-, Q8VU09
absolutely specific for fructose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
specific for fructose 6-phosphate, very low activity with UTP and CTP
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
no activity with glucose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
no activity with glucose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Q9WUA3
sigmoid response to fructose 6-phosphate concentration
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
no cooperativity with respect to fructose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
best phosphoryl donors and acceptors of PFK1 and PFK2
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
reversible reaction in vitro
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
reducing fructose 6-phosphate concentration results in dissociation and inactivation
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
no activity with hexitol 6-phosphates
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
purine NTPs preferred
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
reversible reaction in vivo, but not in vivo, very low activity with acetyl phosphate, UDP and GDP as phosphoryl donors, enzyme is not regulated allosterically
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
sigmoidal kinetics with fructose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
no activity with diphosphate as phosphate donor
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
negative and positive cooperative kinetics at low fructose 6-phosphate concentrations
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
high cooperativity with respect to fructose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
transfers gamma-phosphate of ATP to C-1-hydroxyl of D-(-)fructose 6-phosphate, highly specific for sugar substrate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
transfers gamma-phosphate of ATP to C-1-hydroxyl of D-(-)fructose 6-phosphate, highly specific for sugar substrate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
fructose 6-phosphate shows cooperativity
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
first step in glycolysis
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
allosteric enzyme, involved in regulation of glycolytic flux
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
allosteric enzyme, involved in regulation of glycolytic flux
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
dominant rate-controlling enzyme of glucose degradation via Embden-Meyerhof pathway, involved in generation of glycolytic oscillations
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
50% reduction of PFK expression leads to a proportionally decrease of growth rate, glycolytic flux and lactate flux
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
important control point for glycolytic flux in the pathway from glucose to fatty acid in the lactating mammary gland, PFK is reactivated by re-feeding of starved animals
-
-
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
two types of phosphofructokinase-1 (PFK-L and PFK-M) differentially regulate the glycolytic pathway in insulin-stimulated chicken skeletal muscle
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
importance of phosphofructokinase-M for insulin secretion
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
the enzyme shows cooperative binding for fructose-6-phosphate and non-cooperative binding for ATP. Pfk1 undergoes a large conformational change upon Mg-ATP binding
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
O08333, Q9FC99, Q9L1L8, -
engineering to increase antibiotic production
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
O08333, Q9FC99, Q9L1L8, -
improved antibiotic production by deletion of PFKA2, involvement of PFKA2 in determining the carbon flux distribution
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Aeropyrum pernix DSM 11879
Q9YG89
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Escherichia coli DF1020
-
-, first step in glycolysis
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Escherichia coli DF1020
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Escherichia coli DF1020
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Escherichia coli DF1020
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Aspergillus niger B60
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Entamoeba histolytica H200
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Saccharomyces cerevisiae PS1
P16862
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Schizosaccharomyces pombe CBS1057
-
sigmoidal kinetics with fructose 6-phosphate
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Lactococcus lactis C10
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Oceanimonas doudoroffii M1
-
-
-
?
ATP + D-tagatose 6-phosphate
ADP + ?
show the reaction diagram
-
poor substrate for isoenzyme PFK2
-
-
?
ATP + fructose
ADP + fructose 1-phosphate
show the reaction diagram
-, Q9YG89
-
-
?
ATP + fructose 1-phosphate
ADP + fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + fructose 1-phosphate
ADP + fructose 1,6-bisphosphate
show the reaction diagram
-
60fold lower kcat than with fructose 6-phosphate
-
?
ATP + fructose 1-phosphate
ADP + fructose 1,6-bisphosphate
show the reaction diagram
-
5% of activity with D-fructose 6-phosphate
-
?
ATP + glucose 6-phosphate
ADP + glucose 1,6-bisphosphate
show the reaction diagram
-, Q9YG89
-
-
?
ATP + ribose
ADP + ribose 1-phosphate
show the reaction diagram
-, Q9YG89
-
-
?
ATP + ribose 5-phosphate
ADP + ribose 1,5-bisphosphate
show the reaction diagram
-, Q9YG89
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
P0A796
-
-
-
-
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
-
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
-
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
as effective as ATP
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
less effective than ATP
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
less effective than ATP
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
purine NTPs preferred
-
-
-
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
55% of activity with ATP
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
ITP, GTP or UTP as phosphoryl donors
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
phosphorylation at 28% the rate of ATP
-
-
-
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
13% of activity with ATP
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
Aeropyrum pernix, Aeropyrum pernix DSM 11879
Q9YG89
20.6% of the activity with ATP
-
-
?
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
Oceanimonas doudoroffii M1
-
phosphorylation at 28% the rate of ATP
-
-
-
dATP + D-fructose 6-phosphate
dADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
dATP + D-fructose 6-phosphate
dADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
as good as ATP
-
-
dATP + D-fructose 6-phosphate
dADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
as good as ATP
-
-
gamma-thio-ATP + fructose 6-phosphate
ADP + fructose 1-thio-phosphate-6-phosphate
show the reaction diagram
-
3000fold lower kcat than with ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
P0A796
-
-
-
-
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
-
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
-
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
-
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
purine NTPs preferred
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
42% of activity with ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-, Q8VU09
100% of activity with ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-, Q9YG89
76% of activity with ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
almost as effective as ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
almost as effective as ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
phosphorylation at 35% the rate of ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
less effective than ATP or ITP, better than UTP or CTP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
64% of activity of ATP
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
Aeropyrum pernix, Aeropyrum pernix DSM 11879
Q9YG89
84.1% of the activity with ATP
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
Aspergillus niger B60
-
-
-
-
-
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
Oceanimonas doudoroffii M1
-
phosphorylation at 35% the rate of ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
P0A796
-
-
-
-
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
less effective than ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
less effective than ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
purine NTPs preferred
-
-
-
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-, Q9YG89
76% of activity with ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
phosphorylation at 71% the rate of ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
better than GTP, UTP or CTP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
38% of activity with ATP
-
?
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
130% of activity with ATP
-
?
TTP + D-fructose 6-phosphate
TDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
purine NTPs preferred
-
?
TTP + D-fructose 6-phosphate
TDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
10% of activity with ATP
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
P0A796
-
-
-
-
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
-
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
-
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
as effective as ATP
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
purine NTPs preferred
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-, Q8VU09
40% of activity with ATP
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
less effective than ATP, ITP, GTP, better than CTP
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
phosphorylation at 16% the rate of ATP
-
-
-
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
14% of activity with ATP
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
Oceanimonas doudoroffii M1
-
phosphorylation at 16% the rate of ATP
-
-
-
ITP + D-fructose 6-phosphate
IDP + D-fructose 1,6-bisphosphate
show the reaction diagram
Oceanimonas doudoroffii M1
-
phosphorylation at 71% the rate of ATP
-
?
additional information
?
-
-
insulin may increase the glucose consumption in human erythrocytes, through a mechanism involving Ca2+ influx, calmodulin and the detachment of 6-phosphofructose-1-kinase from the erythrocyte membrane
-
-
-
additional information
?
-
-
structure of the ATP-bound state of phosphofructokinase determined by cryo-electron microscopy
-
-
-
additional information
?
-
-
6-phosphofructokinase is the most important element for control of glycolytic flux
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose 1-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
key enzyme of glucose metabolism
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
P90521
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Q9WUA3
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-, Q8VU09
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-, Q9YG89
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
O08333, Q9FC99, Q9L1L8, -
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
first step in glycolysis
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
allosteric enzyme, involved in regulation of glycolytic flux
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
allosteric enzyme, involved in regulation of glycolytic flux
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
dominant rate-controlling enzyme of glucose degradation via Embden-Meyerhof pathway, involved in generation of glycolytic oscillations
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
50% reduction of PFK expression leads to a proportionally decrease of growth rate, glycolytic flux and lactate flux
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
important control point for glycolytic flux in the pathway from glucose to fatty acid in the lactating mammary gland, PFK is reactivated by re-feeding of starved animals
-
-
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
two types of phosphofructokinase-1 (PFK-L and PFK-M) differentially regulate the glycolytic pathway in insulin-stimulated chicken skeletal muscle
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
importance of phosphofructokinase-M for insulin secretion
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
Escherichia coli DF1020
-
first step in glycolysis
-
?
additional information
?
-
-
insulin may increase the glucose consumption in human erythrocytes, through a mechanism involving Ca2+ influx, calmodulin and the detachment of 6-phosphofructose-1-kinase from the erythrocyte membrane
-
-
-
additional information
?
-
-
6-phosphofructokinase is the most important element for control of glycolytic flux
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
calmodulin binding to the enzyme is stimulated by 0.01 mM Ca2+
Ca2+
P00512
contains Ca2+ ions
Co2+
-
50% of activity with Mg2+-
Co2+
-
12% of activity with Mg+
Co2+
-, Q9YG89
-
Fe2+
-
activation, less effective than Mg2+
Fe2+
-
34% of activity with Mg2+
Fe2+
-
30% of activity with Mg2+
K+
-
kinetics, Km-value: 11.1 mM
K+
-
required for activity, inhibition at high concentrations is reversed by increased concentrations of ATP
K+
-
slight activation at low concentrations
K+
-
activation at low concentrations
K+
-
can replace NH4+; required for activity, inhibition at high concentrations is reversed by increased concentrations of ATP
K+
-
can replace NH4+
K+
-
required for activity, inhibition at high concentrations is reversed by increased concentrations of ATP
K+
-
required for activity, maximal activity at 175 mM, 50% lower activity in the absence of K+
KCl
Q9YG89
optimal activity between 50 and 100 mM. 85% of maximal activity when the KCl concentration is 500 mM
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
Km-values: 0.83-1.1 mM; required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
maximal activity at 5 mM, Km-value: 0.84 mM; MgATP is the active substrate; required for activity
Mg2+
-
required for activity
Mg2+
-
maximal activity approx. above 2 mM; required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate; required for activity; substrate activator and enzyme protein modulator
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate; required for activity
Mg2+
-
MgATP is the active substrate; MgNTP2- is the active substrate; required for activity
Mg2+
Dunaliella marina
-
required for activity
Mg2+
-
Km: 0.5 mM; required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate; required for activity
Mg2+
-
required for activity
Mg2+
-
Km: 0.01 mM; required for activity
Mg2+
-
required for activity
Mg2+
-
MgATP is the active substrate; required for activity
Mg2+
-
required for activity
Mg2+
-
maximal activity at 2-5 mM; required for activity
Mg2+
-
MgATP is the active substrate; required for activity
Mg2+
-
MgATP is the active substrate; required for activity
Mg2+
-
MgATP is the active substrate; required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
1-10 mM are required for maximal activity; required for activity
Mg2+
-
can be partially replaced by Ni2+, Mn2+ and Co2+; required for activity
Mg2+
-, Q8VU09
required for activity
Mg2+
-, Q9YG89
required for activity
Mg2+
-
required for activity
Mg2+
-
required to obtain full activity of the enzyme
Mg2+
-
required for activity
Mg2+
P00512
required
Mg2+
P06999
required for activity, bound to ATP
Mg2+
Q9YG89
the optimal MgCl2 concentration for activity is 20-30 mM and the enzyme possesses 6, 36 and 74% activity compared to the maximal activity when the MgCl2 concentrations are 1.25, 2.5 and 5.0 mM, respectively
Mn2+
-
60% of activity with Mg2+, above 3 mM; activation
Mn2+
-
activation; active substrate: MnATP2-, isoenzyme PFK2; as effective as Mg2+
Mn2+
-
75% of activity with Mg2+; activation
Mn2+
-
activation; as effective as Mg2+
Mn2+
-
24% of activity with Mg2+
Mn2+
-
90% of activity with Mg2+
Mn2+
-, Q9YG89
9% of activity with Mg2+
Ni2+
-
activation, 12% of activity with
Ni2+
-
65% of activity with Mg2+
Ni2+
-, Q9YG89
15% of activity with Mg2+
Zn2+
-
35% of activity with Mg2+; activation
Zn2+
-
activation
Zn2+
-, Q9YG89
46% of activity with Mg2+
Zn2+
-
70% of activity with Mg2+
Mn2+
-
required to obtain full activity of the enzyme. The affinity for Mn2+ is 13fold higher compared to that of Mg2+
additional information
-
not activated by Li+
additional information
-
K-type allosteric enzyme; not activated by Na+ and Rb+
additional information
-
Na+ has little or no effect at 140 nM PFK-1
additional information
-
Cu2+, Zn2+ and Cd2+ do not significantly support the enzymatic activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(-)-Hydroxycitrate
-
-
(NH4)2SO4
-
inhibits above 50 mM
(S)-hexadecyl-CoA
-
-
-
1,3-diphosphoglycerate
-
0.385 mM and 0.005 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition
2',3'-dialdehyde ATP
-
irreversibly modifies a single lysine residue in the ATP-inhibitory site, thereby locking PFK in a permanantly inhibited state without affecting the integrity of the active site
2,3-diphosphoglycerate
-
-
2-oxoglutarate
-
brain PFK, not heart PFK
2-oxoglutarate
-
2 mM, 92% inhibition
2-oxoglutarate
-
competitive inhibition
2-phosphoglycerate
-
2 mM and 3.2 mM, 50% inhibition of cytosolic PFK at pH 8.0 and PH 7.2, respectively, 0.5 mM and 0.4 mM, 50% inhibition of plastid PFK at pH 8.0 and pH 7.2, respectively
2-phosphoglycerate
-
1.3 mM, 50% inhibition of cytosolic PFK, no inhibition in the presence of 5 or 25 mM phosphate
2-phosphoglycerate
Dunaliella marina
-
1 mM, complete inhibition, phosphate relieves, kinetics
2-phosphoglycerate
-
0.032 mM and 0.004 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition
3-phosphoglycerate
-
-
3-phosphoglycerate
-
0.9 mM, 50% inhibition of plastid PFK
3-phosphoglycerate
-
-
3-phosphoglycerate
Dunaliella marina
-
1 mM, complete inhibition, phosphate relieves, 0.5 mM, 50% inhibition, sigmoidal inhibition curve; inhibition kinetics
3-phosphoglycerate
-
2 mM, 86% inhibition; inhibition kinetics
3-phosphoglycerate
-
1.5-2.0 mM, 50% inhibition
3-phosphoglycerate
-
mixed inhibition
3-phosphoglycerate
-
about 70% inhibition at 7 mM
ADP
-
plant enzymes
ADP
-
most potent inhibitor of cytosolic isozyme, 0.4 mM and 4 mM, 50% inhibition of cytosolic and plastid PFK at pH 8.0
ADP
Dunaliella marina
-
-
ADP
-
1.9 mM and 0.0006 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition
ADP
-
complete inhibition at 4.5 mM ADP, 52.4% residual activity at 2.3 mM ADP
ADP
Q9YG89
1 mM, 82% inhibition
ammonium sulfate
-, Q9YG89
50 mM, 50% inhibition
AMP
-
5 mM, 80% inhibition
AMP
-
at high fructose 6-phosphate concentrations, activates at low fructose 6-phosphate concentrations
AMP
-, Q8VU09
1 mM and 4 mM, 20% and 40% inhibition in the presence of 5 mM fructose 6-phosphate and Mg2+
Antibodies against rabbit muscle enzyme
-
not rabbit erythrocyte, leukocyte or platelet enzyme
-
Arachidonoyl-CoA
-
-
arginine phosphate
-
-
ascorbate
-
inhibition by ascorbate is PFK-1 concentration dependent. Ascorbate does not inhibit above 200 nM PFK-1. It is concluded that ascorbate inhibits PFK-1 dimers (and perhaps monomers) but not PFK-1 tetramers
ATP
-
ADP partially reverses inhibition
ATP
-
ADP partially reverses inhibition; cAMP partially reverses inhibition; fructose 1,6-bisphosphate partially reverses inhibition; phosphate and AMP partially reverse inhibition
ATP
-
muscle PFK, strong inhibition at pH 7.1, weak inhibition at pH 7.6-8.5, not inhibited at pH 9.0
ATP
-
fructose 1,6-bisphosphate partially reverses inhibition; phosphate and AMP partially reverse inhibition
ATP
-
at high concentrations
ATP
-
cytosolic isoenzyme is more sensitive to inhibition at pH 8.0 than pH 7.2, Mg2+ alleviates inhibition
ATP
-
at high concentrations
ATP
-
pH-dependent inhibition
ATP
-
cAMP partially reverses inhibition; fructose 6-phosphate partially reverses inhibition; pH-dependent inhibition; phosphate and AMP partially reverse inhibition
ATP
-
above 1 mM, inhibition is relieved by Mg2+; free form
ATP
-
inhibition of plastid PFK above 5 mM at pH 8.0 and above 0.5 mM at pH 7.2
ATP
-
2 mM, 50% inhibition of cytosolic PFK at pH 8.0, 5 mM, 50% inhibition of plastid PFK at pH 8.0
ATP
-
substrate inhibition
ATP
Dunaliella marina
-
strong inhibition above 1 mM, at 2.5 mM Mg2+
ATP
-
above 0.2 mM, inhibition is alleviated by Mg2+; free form
ATP
-
fructose 6-phosphate partially reverses inhibition
ATP
-
1 mM, almost complete inhibition of native PFK, phosphorylated PFK is less sensitive to inhibition
ATP
-
at high concentrations
ATP
-
ADP partially reverses inhibition; fructose 6-phosphate partially reverses inhibition; phosphate and AMP partially reverse inhibition
ATP
-
above 0.05 mM, inhibition is more pronounced at pH 6.6 but occurs also at pH 8.0, inhibition is reversed by equivalent amounts of AMP
ATP
-
NaF and limited proteolysis protect from inhibition
ATP
-
0.99 mM, 50% inhibition
ATP
-
7.5 mM, 98% inhibition; fructose 2,6-bisphosphate partially reverses inhibition
ATP
-
0.004 mM and 0.003 mM, 50% inhibition at 20C and 6C, respectively, normoxic turtles
ATP
-
fructose 2,6-bisphosphate partially reverses inhibition; phosphate and AMP partially reverse inhibition
ATP
-
synergistic with citrate
ATP
-
above 1 mM at 0.33 mM fructose 6-phosphate and 2 mM Mg2+, inhibition at a Mg/ATP ratio below 2; ADP partially reverses inhibition; fructose 6-phosphate partially reverses inhibition; Mg2+ partially reverses inhibition
ATP
-
1 mM, 90% inhibition of the activity observed with 0.1 mM ATP
ATP
-
at alkaline pH; mechanism
ATP
-
above 0.25 mM in the absence of MgCl2; free form
ATP
-
0.02 mM and 0.94 mM, 50% inhibition at 0.0001 mg/ml and at 0.0006 mg/ml PFK respectively, 3.23 mM, 50% inhibition at 0.0006 mg/ml PFK in the presence of 10% polyethylene glycol
ATP
-
inhibition of M-type PFK above 0.1 mM
ATP
-
in the absence of AMP and fructose 2,6-bisphosphate
ATP
-
inhibition above 0.08 mM
ATP
-
0.4 mM, 50% inhibition of PFK C
ATP
-
lower inhibition at pH 6.6 compared to pH 7.2
ATP
-
inhibition of fructose 1-phosphate phosphorylation above 0.08 mM ATP
ATP
-
potentiates inhibitory action of citrate
ATP
-
at physiological concentration; at physiological pH, the enzyme is allosterically inhibited by near-physiological concentrations of its co-substrate ATP, which induces cooperativity, i.e. reduces the affinity for the substrate fructose 6-phosphate. Inhibition by ATP is reinforced by citrate and H+
ATP
-
the inhibition of enzyme activity by ATP (above 1 mM) is abolished in the presence of calmodulin
ATP
-
complete inhibition at 10 mM
ATP
P78985
in contrast to the native PFK1 enzyme, the 49 kDa PFK1 fragment is highly sensitive to ATP inhibition (5fold lower activity at the 1 mM ATP than at the 0.1 mM concentration)
ATP
-
allosteric inhibition by high ATP concentrations. The inhibitory effects of high ATP concentration can be reversed by D-fructose 2,6-bisphosphate and AMP
ATP
-
millimolar inhibitor
aurintricarboxylic acid
-
0.0002 mM, 50% inhibition at pH 7.3, reversed by addition of allosteric activators, i.e., fructose 2,6-bisphosphate or AMP, no inhibition at pH 8.0
Ca2+
-
depending upon total Mg2+-concentration, kinetics, cytosolic isozyme
Ca2+
-
competitive vs. Mg2+
cis-aconitate
-
brain, not heart
citrate
-
strong inhibition; synergistic with phosphate and AMP
citrate
-
weak inhibition
citrate
-
at pH 7.6, not at pH 8.4
citrate
-
10 mM, approx. 30% inhibition
citrate
-
10 mM, 60% inhibition
citrate
Dunaliella marina
-
-
citrate
-
2 mM, complete inhibition
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
weak inhibition
citrate
-
strong inhibition; weak inhibition
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
isoenzyme PFK2
citrate
-
0.12 mM, 50% inhibition
citrate
-
with glucose 1,6-bisphosphate or fructose 1,6-bisphosphate as activator
citrate
-
0.23 and 0.17 mM mM, 50% inhibition at 20 and 6C, respectively, normoxic turtles, 0.3 mM, 50% inhibition at 20C and 6C, anoxic turtles
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
strong inhibition; synergistic with ATP; synergistic with NH4+; synergistic with phosphate and AMP
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
weak inhibition
citrate
-
cAMP, ADP or fructose 1,6-bisphosphate restore activity
citrate
-
inhibition of M- and C-type PFK in pancreatic beta-cells
citrate
-
presence of 12 mM Mg2+ relieves inhibition completely
citrate
Q9WUA3
-
citrate
-
50% inhibition below 0.25 mM
citrate
-
the native 85000 Da enzyme is moderately inhibited by citrate, the 49000 Da shorter fragment of PFK1 proves to be completely resistant to inhibition by citrate
citrate
-
almost complete inhibition at 1 mM citrate in the absence of D-fructose 2,6-bisphosphate
citrate
P78985
when 5 mM of citrate is added a moderate reduction for about 1020% is recorded in the homogenate of TE22 and TE23 strain, while in A158 strain much stronger reduction of PFK1 specific activity, for approximately 40% is observed
citrate
-
mild inhibitory effects, but only at concentrations exceeding 2 mM
citrate
-
activates the enzyme in the absence of phosphate and inhibits the enzyme in the presence of phosphate
clotrimazole
-
clotrimazole alone induces dimerization of the enzyme reducing the population of tetramers, which is not observed when calmodulin is also present. Since PFK dimers are less active than tetramers, this can explain the inhibitory effect of clotrimazole
CTP
-
free form, Mg2+ relieves
Cu2+
-
0.001 mM, 28% inhibition
Cu2+
Q9YG89
1 mM, 52.4% inhibition
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
product inhibition
D-fructose 1,6-bisphosphate
-
0.02 mM, 50% inhibition in the presence of physiological concentrations of ATP, AMP, phosphate and fructose 6-phosphate
D-fructose 1,6-bisphosphate
-
5 mM, 25% inhibition
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
0.02 mM, 50% inhibition at 100 mM fructose 6-phosphate in the absence of fructose 2,6-bisphosphate, inhibition is reversed by fructose 2,6-bisphosphate
D-fructose 1,6-bisphosphate
-
in the absence of fructose 2,6-bisphosphate
D-fructose 6-phosphate
P06999
inhibition occurs at low concentrations of fructose 6-phosphate
D-Glucose 1,6-bisphosphate
-
0.08 mM, 50% inhibition in the presence of physiological concentrations of ATP, AMP, phosphate and fructose 6-phosphate, inhibition is relieved by 50% by 0.008 mM fructose 2,6-bisphosphate
D-Glucose 1,6-bisphosphate
-
in the absence of fructose 2,6-bisphosphate
D-glucose 6-phosphate
Dunaliella marina
-
weak inhibition
diphosphate
-
inactivates under assay conditions
diphosphate
-
0.1 mM, 80% inhibition, nucleotide diphosphates, i.e. ADP, GDP or TDP, partially alleviate inhibition
diphosphate
-, Q8VU09
1 mM and 4 mM, 20% and 50% inhibition in the presence of 5 mM fructose 6-phosphate and 5 mM Mg2+
diphosphate
Q9YG89
1 mM, 21% inhibition
Dithionitrobenzoic acid
-
0.06 mM, 80% inhibition of PFK III, reversed by 2-mercaptoethanol, dithiothreitol or reduced glutathione
GDP
Q9YG89
1 mM, 46% inhibition
GDP
-
activates the enzyme in the absence of phosphate and inhibits the enzyme in the presence of phosphate
GTP
-
free form, Mg2+ relieves
GTP
-
plastid, not cytosolic, isozyme
Isocitrate
-
brain, not heart
Isocitrate
-
competitive inhibition
Isocitrate
-
mild inhibitory effects, but only at concentrations exceeding 2 mM
K+
-
at high concentrations, ATP reverses
K+
-
about 30% residual activity of 30 nM PFK-1 in the presence of 0.2 M K+
KCl
-, Q9YG89
100 mM, 50% inhibition
KCl
-
inhibits above 50 mM
Lactate dehydrogenase
-
lactate dehydrogenase suspended in 3.2 M ammonium sulfate inhibits 30 nM PFK-1 resulting in a more than 50% inhibition of activity
-
Li2CO3
-
about 75% residual activity at 20 mM, about 40% residual activity at 40 mM, about 10% residual activity at 100 mM, less than 3% residual activity at 200 mM
-
Li2SO4
-
about 55% residual activity at 100 mM, about 30% residual activity at 200 mM
lithium acetate
-
about 80% residual activity in the presence of 0.009 mM lithium acetate
-
malate
-
kidney cortex, brain, not heart
malate
-
2 mM, 92% inhibition
malate
-
competitive inhibition
malate
-
mild inhibitory effects, but only at concentrations exceeding 2 mM
Maleic anhydride
-
muscle and heart enzymes, mechanism
Mg2+
-
brain enzyme, at high concentrations
Mg2+
-
free form, citrate reverses, independent of MgATP-concentration, kinetics, cytosolic isozyme
MgATP2-
-
cytosolic isozyme
Na+
-
about 70% residual activity of 30 nM PFK-1 in the presence of 0.2 M Na+
NaCl
-, Q9YG89
1 M, 50% inhibition
NH4+
-
muscle PFK, weak, at high concentrations, activation at very low concentrations
NH4+
-
about 40% residual activity of 30 nM PFK-1 in the presence of 0.2 M NH4+
nucleoside triphosphate
-
-
nucleoside triphosphate
-
free form, pH-dependent
nucleoside triphosphate
-
at a Mg/NTP ratio below 2
p-Chloromercurisulfonic acid
-
0.025 mM, 80% inhibition of PFK III, reversed by 2-mercaptoethanol, dithiothreitol or reduced glutathione
palmitoyl-CoA
-
low micromolar inhibitor, MgAMP and MgADP but not MgATP protect the enzyme against inhibition by palmitoyl-CoA. Acyl-protein thioesterase-1 reverses palmitoyl-CoA-mediated enzyme inhibition
palmitoylcarnitine-CoA
-
-
-
phosphatase
-
dephosphorylation inactivates
-
phosphate
-
inhibition at 10-100 mM, concentrations at 1- 5 mM relieve the influence of other inhibitors such as phosphoenolpyruvate
phosphate
-
weak
phosphate
Dunaliella marina
-
above 5 mM; kinetics; the enzyme is both activated and inhibited by phosphate, depending on fructose 6-phosphate/phosphate-ratio
phosphate
-
10 mM, 50% inhibition
phosphate
-
25 mM, 50% and 57% inhibition of PFK-1 at pH 6.6 and pH 7.2, respectively
phosphate
A1XM06, A1XM07, -
slight inhibition; slight inhibition; slight inhibition
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
at pH 7.6, not at pH 8.4
phosphoenolpyruvate
-
0.1 mM, 50% inhibition at low pH; phosphate relieves
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
1 mM, approx. 75% inhibition
phosphoenolpyruvate
-
0.05 mM, 50% inhibition of plastid PFK
phosphoenolpyruvate
-
0.04 mM and 0.05 mM, 50% inhibition of plastid PFK at pH 8.0 and pH 7.2, respectively; most potent inhibitor
phosphoenolpyruvate
-
0.22 mM, 50% inhibition of cytosolic PFK in the presence of 1 mM fructose 6-phosphate, phosphate relives inhibition
phosphoenolpyruvate
Dunaliella marina
-
1 mM, complete inhibition, 0.08 mM, 50% inhibition; inhibition kinetic; phosphate relieves
phosphoenolpyruvate
-
2 mM, complete inhibition; inhibition kinetic
phosphoenolpyruvate
-
inhibition kinetic
phosphoenolpyruvate
-
effective inhibition at 0.005-0.02 mM, fructose 6-phosphate relieves inhibition; most potent inhibitor
phosphoenolpyruvate
-
most potent inhibitor
phosphoenolpyruvate
-
5 mM; 64% inhibition
phosphoenolpyruvate
-
0.59 mM, 50% inhibition
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
feedback inhibition
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
inhibition of mammary gland PFK
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
0.1 mM and 10 mM, allosteric inhibition, almost completely reversed by 2.5 mM ADP
phosphoenolpyruvate
-
0.0023 mM and 0.0009 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition
phosphoenolpyruvate
-
mixed inhibition
phosphoenolpyruvate
-
about 30% inhibition at 5 mM
phosphoenolpyruvate
-
-
Phosphoglycolate
-
0.25 mM, 50% inhibition of plastid PFK
Phosphoglycolate
Dunaliella marina
-
1 mM, complete inhibition, phosphate relieves, kinetics
Phosphoglycolate
-
0.006 mM and 0.003 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition
Protein factor
-
19000 Da protein promotes Zn2+ or Fe2+-dependent dissociation into inactive protomers, maximal inactivation at 0.001-0.02 mM Zn2+, inactivation is abolished at higher Zn2+ concentrations, Ca2+, Mg2+, Mn2+ can substitute for Zn2+ or Fe2+ only at millimolar concentrations, potency in descending order: Mn2+, Mg2+, Ca2+, inactivation can be reversed by the addition of ATP, fructose 1,6-bisphosphate, or fructose 2,6-bisphosphate
-
pyridoxal 5'-phosphate
-
muscle and heart enzymes, mechanism
SO42-
-
20 mM, 50% inhibition of cytosolic and 77% inhibition of plastid PFK at pH 7.2, not at pH 8.0
SO42-
-
2 mM, 50% inhibition at pH 7.2, 5 mM complete inhibition
succinate
-
kidney cortex and brain PFK, heart PFk is not inhibited
succinate
-
competitive inhibition
Succinic anhydride
-
muscle and heart enzymes, mechanism
UTP
-
free form, Mg2+ relieves
Zn2+
-
0.001 mM, 28% inhibition
MgATP2-
P06999
inhibition occurs at high concentrations of MgATP2-
additional information
-
not inhibited by ATP; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by ATP; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by ATP; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA; photooxidation yields a new heart enzyme species that is no longer sensitive to ATP
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA; photooxidation yields a new heart enzyme species that is no longer sensitive to ATP
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
heart enzyme, not inhibited by cis-aconitate, L-isocitrate, alpha-ketoglutarate, succinate, fumarate, malate, tricarnallylic acid, CoASH, or acetyl-CoASH; not inhibited by fructose 1,6-bisphosphate; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA; photooxidation yields a new heart enzyme species that is no longer sensitive to ATP
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by GTP; not inhibited by ITP, fumarate, tricarballylic acid, CoA, acetyl-CoA
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by MgATP2-
-
additional information
-
not inhibited by fructose 6-phosphate
-
additional information
-
not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by MgATP2-
-
additional information
-
not inhibited by AMP; not inhibited by cAMP; not inhibited by phosphate
-
additional information
-
cytosolic PFK is not inhibited by GTP; not inhibited by fructose 2,6-bisphosphate
-
additional information
-
cytosolic PFK is not inhibited by ATP and SO42-
-
additional information
-
not inhibited by 3-phosphoglycerate; not inhibited by fructose 2,6-bisphosphate; not inhibited by Na+
-
additional information
-
not inhibited by cAMP; not inhibited by UDP, UDPglucose
-
additional information
Dunaliella marina
-
not inhibited by ADPglucose, dithiothreitol, gluconate 6-phosphate, glucose 1-phosphate; not inhibited by NH4+ and K+
-
additional information
-
not inhibited by 2-phosphoglycerate; not inhibited by fructose 2,6-bisphosphate; not inhibited by glutamine, glutamate
-
additional information
-
not inhibited by AMP
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by fructose 2,6-bisphosphate; not inhibited by phosphate
-
additional information
-
not inhibited by ADP; not inhibited by Ca2+; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
effect of low temperature or anoxia on inhibition kinetics
-
additional information
-
not inhibited by cAMP
-
additional information
-
not inhibited by phosphate
-
additional information
-
not inhibited by ADP
-
additional information
-
product inhibition of reverse reaction
-
additional information
-
not inhibited by ATP
-
additional information
-
not inhibited by fructose 1,6-bisphosphate; not inhibited by pyruvate; not inhibited by ribulose 5-phosphate
-
additional information
-
not inhibited by 2-phosphoglycerate; not inhibited by 3-phosphoglycerate; not inhibited by ADP; not inhibited by fructose 1,6-bisphosphate
-
additional information
-
not inhibited by AMP; not inhibited by cAMP; not inhibited by phosphate; not inhibited by pyruvate
-
additional information
-
no substrate inhibition with gamma-thio-ATP
-
additional information
-
high insulin concentration decreases enzyme activity in intact cells
-
additional information
-
not inhibited by 6-phosphogluconate and phosphocreatine
-
additional information
P78985
the active 49 kDa PFK1 fragment is not inhibited by citrate
-
additional information
-
not inhibited by ATP
-
additional information
-
acetyl-CoA, malonyl-CoA, palmitoylcarnitine, and palmitic acid in the presence of CoASH are without effect on enzyme activity
-
additional information
-
not inhibited by LiCl
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-
activation
ADP
-
activation
ADP
-
1.8 mM, half-maximal activation at fructose 6-phosphate concentrations below 0.5 mM
ADP
-
activation
ADP
-
activation; slight
ADP
-
activation; at high fructose 6-phosphate concentration, inhibits at low fructose 6-phosphate concentration
ADP
-
activation; positive effector
ADP
-
activation; positive effector
ADP
-
activates
Aldolase
-
about 120% activity in the presence of 0.005 mM aldolase
-
AMP
-
activation
AMP
-
activation
AMP
-
0.64 mM, half-maximal activation at fructose 6-phosphate concentrations below 0.5 mM
AMP
-
activation; one of three most potent activators
AMP
-
activation; synergistic with fructose 2,6-bisphosphate
AMP
-
activation; positive effector
AMP
-
activation; concomitant with NH4+ and phosphate
AMP
-
activation at low fructose 6-phosphate concentrations, inhibition at high fructose 6-phosphate concentrations
AMP
-
2-5 mM, maximal activation at 3 mM ATP
AMP
-
activation follows a saturation function, Km: 0.56 mM
AMP
-
activates 85000 Da native enzyme form and the 49000 Da shorter fragment
AMP
-
activates
AMP
-
activates; at near-physiological substrate concentrations, PFK activity requires activators of which the combination of AMP and fructose 2,6-bisphosphate is most efficient as a result of synergistic effects
Calmodulin
-
clotrimazole-inhibited enzyme can be activated by calmodulin
Calmodulin
-
binding of one calmodulin per monomer promotes the dimerization of the enzyme although maintaining its full catalytic activity, 30 nM calmodulin activates 6-phosphofructo-1-kinase in the presence of its inhibitors citrate and lactate
cAMP
-
activation
cAMP
-
0.4 mM, half-maximal activation at fructose 6-phosphate concentrations below 0.5 mM
cAMP
-
activation
cAMP
-
0.1 mM, approx. 5fold activation
cAMP
-
0.1 mM, activates
cAMP-dependent protein kinase
-
activation by phosphorylation
-
cAMP-dependent protein kinase
-
activation by phosphorylation; kinetics, one of three most potent activators
-
citrate
-
stimulation, by chelating of free Mg2+
citrate
-
activates the enzyme in the absence of phosphate and inhibits the enzyme in the presence of phosphate
Cl-
-
200 mM, 3.1fold activation of cytosolic PFK
D-fructose 1,6-bisphosphate
-
activation
D-fructose 1,6-bisphosphate
-
activation
D-fructose 1,6-bisphosphate
-
activation
D-fructose 1,6-bisphosphate
-
activation
D-fructose 1,6-bisphosphate
-
half-maximal activation at 0.0035 mM
D-fructose 1,6-bisphosphate
-
activation; activation of flight muscle PFK in the absence of fructose 2,6-bisphosphate
D-fructose 1,6-bisphosphate
-
activation of PFK in INS-1 cell extract
D-fructose 2,6-bisphosphate
-
activation of native and phosphorylated PFK, one of three most potent activators
D-fructose 2,6-bisphosphate
-
3fold activation in the presence of approx. 0.003 mM, i.e. the physiological fructose 2,6-bisphosphate concentration; synergistic with AMP
D-fructose 2,6-bisphosphate
-
strong positive allosteric action on PFK
D-fructose 2,6-bisphosphate
-
activation
D-fructose 2,6-bisphosphate
-
activation
D-fructose 2,6-bisphosphate
-
activation of PFK in INS-1 cell extract
D-fructose 2,6-bisphosphate
-
approx. 200-400 mM, maximal activation at 3 mM ATP
D-fructose 2,6-bisphosphate
-
strong stimulation of mammary gland PFK, Kact: 0.00005 mM
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
Q9WUA3
-
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
half-maximal activation at 0.0003 mM
D-fructose 2,6-bisphosphate
-
cooperative activation, Km: 0.00023 mM
D-fructose 2,6-bisphosphate
-
activates at concentrations above 0.002 mM
D-fructose 2,6-bisphosphate
-
activates
D-fructose 2,6-bisphosphate
-
converts saturation curves for D-fructose 6-phosphate to hyperbolic and activates PFK synergistically with AMP
D-fructose 2,6-bisphosphate
P78985
the active 49 kDa PFK1 fragment is activated to a higher level by D-fructose 2,6-bisphosphate with respect to the native enzyme, a significant boost in the enzyme activity of the fragment is registered at 1 mM ATP after the introduction of 0.004 mM of D-fructose-2,6-bisphosphate
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
P16862
-
D-fructose-1,6-bisphosphate
-
activates synergistically with AMP and ADP
D-Glucose 1,6-bisphosphate
-
activation
D-Glucose 1,6-bisphosphate
-
-
D-Glucose 1,6-bisphosphate
-
activation
D-Glucose 1,6-bisphosphate
-
activation only in the presence of AMP
D-Glucose 1,6-bisphosphate
-
half-maximal activation at 0.013 mM
D-Glucose 1,6-bisphosphate
-
0.02 mM, 474% and 360% activation of M- and L-type PFK, respectively
D-glucose 6-phosphate
-
4.8 mM, 1.5fold increase in activity at 2 mM fructose 6-phosphate, 2fold increase at 4 mM fructose 6-phosphate, in vitro
Dimethylsulfoxide
-
20%, 9fold increase in activity, probably due to crowding effect
fructose 2,6-bisphosphate
-
at near-physiological substrate concentrations, PFK activity requires activators of which the combination of AMP and fructose 2,6-bisphosphate is most efficient as a result of synergistic effects
GDP
-
activation
GDP
-
activation at low concetrations, inhibition above 1 mM
GDP
-
activates the enzyme in the absence of phosphate and inhibits the enzyme in the presence of phosphate
glutathione
-
activation
glycerol
-
40%, 4fold increase in activity, probably due to crowding effect
HAsO42-
-
50 mM, 2.9fold activation of cytosolic PFK
HCO3-
-
200 mM, 2.1fold activation of cytosolic PFK
NH4+
-
activation of muscle enzyme, inhibitory at high concentrations
NH4+
-
40 mM, 50% activation at pH 8.0 and pH 7.2
NH4+
-
cytosolic isozyme is not activated
NH4+
-
at very low concentration, kinetics, Km-value: 0.56 mM
NH4+
-
increases maximum activity of PFK and the affinity of PFK to fructose 6-phosphate
NH4+
-
activation at low concentrations
NH4+
-
concomitant with AMP and phosphate
NH4+
-
NH4+ increases the affinity for fructose 6-phosphate, counteracts the inhibition by ATP
NH4+
-
can replace K+; required for activity
NH4+
-
can replace K+
NH4+
-
required for activity
NH4+
-
activates
NO3-
-
50 mM 1.6fold activation of cytosolic PFK
phosphate
-
activation of cytosolic and plastidic isoenzyme
phosphate
-
1 mM, strong activtion of plastid PFK at pH-values below 7.0; cytosolic isozyme: slight activation
phosphate
-
25 mM, 3.2fold activation of cytosolic PFK
phosphate
Dunaliella marina
-
kinetics; the enzyme is both activated and inhibited by phosphate, depending on fructose 6-phosphate/phosphate-ratio
phosphate
-
25% activation at 5 mM, inhibition above
phosphate
-
kinetics, Km-value: 1.64 mM
phosphate
-
synergistic with AMP
phosphate
-
concomitant with NH4+ and AMP
phosphate
-
activates
Polyethylene glycol
-
20%, 8fold increase in activity, probably due to crowding effect
SO42-
-
50 mM, 2.6fold activation of cytosolic PFK
SO42-
-
kinetics, Km-value: 1.73 mM; stimulation
SO42-
-
stimulation
Sodium acetate
-
about 115% activity in the presence of 0.04 mM sodium acetate
trehalose
-
activates
MgATP2-
P06999
the apparent Km for MgATP2- is 0.022 mM
additional information
-
not activated by fructose 2,6-bisphosphate
-
additional information
-
effector studies at near-physiological conditions
-
additional information
-
allosteric enzyme
-
additional information
-
allosteric enzyme; K-type allosteric enzyme
-
additional information
-
not activated by 2-oxoglutarate
-
additional information
-
-
-
additional information
-
ascites tumor PFK is not activated by fructose-1,6-bisphosphate
-
additional information
-
addition of oestradiol increases enzyme activity in intact cells
-
additional information
-
not activated by D-fructose 2,6-bisphosphate
-
additional information
-
D-glucose 1,6-bisphosphate and phosphoenolpyruvate have no effect on activity
-
additional information
-
not influenced by potassium acetate
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1
-
adenosine
-, Q9YG89
pH 6.7, 85C
0.49
-
ADP
-
pH 6.0, 85C
1.4
-
ADP
-
pH 7.0, 75C
0.005
-
ATP
-
pH 7.2, 25C, cytosolic PFK
0.006
-
ATP
-
pH 7.2, 25C, plastid PFK
0.007
-
ATP
-
pH 8.0, 25C, cytosolic PFK
0.008
-
ATP
-
wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.0087
-
ATP
-
pH 7.0, 25C, cytosolic PFK
0.009
-
ATP
-
pH 7.7
0.009
-
ATP
-
pH 7.25, 25C
0.009
-
ATP
-
pH 7.8, 50C
0.01
-
ATP
-
pH 7.0
0.012
-
ATP
-
wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.013
-
ATP
-
pH 7.0, 25C, chloroplasr PFK
0.013
-
ATP
-
pH 6.7, 37C, at 0.25 mM fructose 6-phosphate
0.014
-
ATP
-
pH 8.0, 25C, plastid PFK
0.0151
-
ATP
-
mutant enzyme N341A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.017
-
ATP
-
pH 6.7, 37C, at 0.4 mM fructose 6-phosphate
0.017
-
ATP
-
wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25C
0.02
-
ATP
-
pH 7.2, 30C, cosubstrate fructose 1-phosphate
0.021
-
ATP
-
pH 7.3, 25C, PFK II
0.022
-
ATP
-
-
0.022
-
ATP
-
pH 6.8, 30C
0.023
-
ATP
-
pH 6.7, 37C, at 0.75 mM fructose 6-phosphate
0.023
-
ATP
-
pH 7.0, 6C, normoxic animals
0.0232
-
ATP
-
mutant enzyme N341A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.025
-
ATP
-
pH 8.0
0.026
-
ATP
-
pH 6.7, 37C, at 2.0 mM fructose 6-phosphate
0.027
-
ATP
-
pH 7.2, 25C
0.027
-
ATP
Q9YG89
pH 6.5, 95C, discontinuous assay
0.0275
-
ATP
-
mutant enzyme S377A/K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.028
-
ATP
-
pH 8.0, 25C, cytosolic PFK
0.03
-
ATP
-
pH 7.2, 22C
0.03
-
ATP
-
pH 7.0, 6C, anoxic animals
0.0326
-
ATP
-
mutant enzyme K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.0338
-
ATP
-
mutant enzyme H242A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.034
-
ATP
-
pH 7.0, 20C, normoxic and anoxic animals
0.034
-
ATP
-
pH 8.0, 25C, PFK I
0.0356
-
ATP
-
mutant enzyme K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; mutant enzyme N341A/R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.037
-
ATP
-
mutant enzyme S377A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.0382
-
ATP
-
mutant enzyme H242A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.0384
-
ATP
-
mutant enzyme K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.039
-
ATP
-
pH 8.0, 30C
0.04
-
ATP
-
pH 7.5
0.0415
-
ATP
-
mutant enzyme S377A/K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.0425
-
ATP
-
wild type enzyme, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.0425
-
ATP
-
mutant enzyme R246A/K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; wild type enzyme, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.043
-
ATP
-
mutant enzyme S377A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.0432
-
ATP
-
mutant enzyme R246A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.0477
-
ATP
-
mutant enzyme R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.049
-
ATP
-
mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.0498
-
ATP
-
wild type enzyme, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.05
-
ATP
-
pH 8.4
0.05
-
ATP
-
pH 7.9, 24C
0.05
-
ATP
-
pH 8.2, 28C, PFK2
0.0508
-
ATP
-
mutant enzyme R246A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.051
-
ATP
-
purified enzyme, at pH 7.0, in the absence of D-fructose 2,6-bisphosphate
0.0524
-
ATP
-
mutant enzyme K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.0528
-
ATP
-
mutant enzyme N341A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.055
-
ATP
-
pH 8.0, 28C
0.055
-
ATP
-
pH 8.5, 30C, I126A mutant PFK; pH 8.5, 30C, wild-type PFK
0.055
-
ATP
-
-
0.06
-
ATP
Dunaliella marina
-
pH 7.0
0.06
-
ATP
-
PFK-1
0.063
-
ATP
-
mutant enzyme N341A/R246A/K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.0647
-
ATP
-
mutant enzyme D543A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.0674
-
ATP
-
mutant enzyme D543A, in the presence of 1 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; mutant enzyme D543A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.07
-
ATP
-
pH 6.8, 30C
0.07
-
ATP
-
wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25C
0.076
-
ATP
-
purified enzyme, at pH 7.0, in the presence of 0.005 mM D-fructose 2,6-bisphosphate
0.0769
-
ATP
-
mutant enzyme D543A, in the presence of 0.1 mM 5-phospho-alpha-D ribose 1-diphosphate, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.08
-
ATP
-
pH 7.8, 30C
0.081
-
ATP
A1XM06, A1XM07, -
; 30C, pH 7.8; 30C, pH 7.8
0.0894
-
ATP
-
mutant enzyme D543A, in the presence of 0.1 mM 2'-iodo-ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.094
-
ATP
-
pH 8.5, 30C, R72H mutant PFK
0.1
-
ATP
-
pH 6.0, 50C
0.1
-
ATP
-
12 h after isoproterenol administration, PFK-1
0.1
-
ATP
-
pH 7.2, 30C
0.11
-
ATP
-
pH 8.5, 30C, wild-type PFK
0.114
-
ATP
-
mutant enzyme D543A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.114
-
ATP
-
mutant enzyme H242A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.117
-
ATP
-
mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.12
-
ATP
-
pH 8.0, 25C, erythrocyte PFK
0.12
-
ATP
-
pH 8.2, 30C, native PFK
0.13
-
ATP
-
pH 8.2, 30C, G212V mutant PFK
0.14
-
ATP
-
pH 8.0, 25C
0.14
-
ATP
-
pH 8.0, 28C
0.141
-
ATP
-
mutant enzyme S377A/K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.151
-
ATP
-
mutant enzyme N341A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.166
-
ATP
-
mutant enzyme R246A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.168
-
ATP
-
mutant enzyme K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; mutant enzyme S377A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.169
-
ATP
-
mutant enzyme D543A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; wild type enzyme, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.169
-
ATP
-
wild type enzyme, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.2
-
ATP
-
pH 7.0, 50C and 75C
0.2
-
ATP
-
pH 8.5, 30C
0.21
-
ATP
-
pH 7.2, 30C
0.22
0.28
ATP
-
-
0.22
0.28
ATP
-
-
0.22
-
ATP
-
mutant enzyme N341A/R246A/K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.23
0.28
ATP
-
pH 7.0, 25, 37C and 50C
0.23
-
ATP
-
-
0.234
-
ATP
-
mutant enzyme R246A/K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.25
-
ATP
-, Q9YG89
pH 6.7, 85C
0.25
-
ATP
-
mutant enzyme K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.28
-
ATP
-
pH 6.0, 85C
0.6
0.9
ATP
-, Q8VU09
pH 7.5, 37C
0.7
-
ATP
-
pH 7.9
0.018
-
CTP
-
pH 8.0, 25C, cytosolic PFK
0.019
-
CTP
-
pH 7.2, 25C, plastid PFK
0.021
-
CTP
-
pH 7.2, 25C, cytosolic PFK
0.03
-
CTP
-
pH 7.3, 25C, PFK II
0.033
-
CTP
-
pH 8.0, 25C, plastid PFK
0.099
-
CTP
-
pH 8.0, 25C, PFK I
11
-
CTP
-
pH 7.2, 30C
7.6
-
D-fructose 1,6-bisphosphate
-
pH 7.0, 75C
16.7
-
D-fructose 1,6-bisphosphate
-
pH 6.0, 85C
0.007
-
D-fructose 6-phosphate
-
mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication; mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.011
-
D-fructose 6-phosphate
-
pH 8.2, 28C, PFK2
0.018
-
D-fructose 6-phosphate
-
wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.019
-
D-fructose 6-phosphate
-
-
0.023
-
D-fructose 6-phosphate
-
pH 7.0 and pH 8.0
0.023
-
D-fructose 6-phosphate
-
pH 8.2, 30C, native PFK
0.024
-
D-fructose 6-phosphate
-
-
0.026
-
D-fructose 6-phosphate
-
pH 8.2, 30C, G212V mutant PFK
0.028
-
D-fructose 6-phosphate
-
pH 8.2, 30C, cosubstrate GTP
0.03
-
D-fructose 6-phosphate
-
pH 8.2, 30C, at fructose 6-phosphate concentrations that are less than approx. one-third the fixed MgATP concentration
0.037
-
D-fructose 6-phosphate
-
wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.043
-
D-fructose 6-phosphate
-
pH 7.0, 6C, normoxic animals
0.047
-
D-fructose 6-phosphate
-
pH 7.1, 25C, M-type PFK
0.05
-
D-fructose 6-phosphate
-
pH 6.8, 30C
0.05
-
D-fructose 6-phosphate
-
-
0.068
-
D-fructose 6-phosphate
-
pH 8.2, 30C, cosubstrate UTP
0.071
-
D-fructose 6-phosphate
-
-
0.086
-
D-fructose 6-phosphate
-
-
0.095
-
D-fructose 6-phosphate
-
pH 7.0, 6C, anoxic animals
0.096
-
D-fructose 6-phosphate
-
pH 7.2, 30C, cosubstrate gamma-thio-ATP
0.106
-
D-fructose 6-phosphate
-
pH 7.0, 20C, anoxic animals
0.11
-
D-fructose 6-phosphate
-
pH 7.0, 20C, normoxic animals
0.14
-
D-fructose 6-phosphate
-
pH 8.5, 30C, D127/R252Q double mutant PFK
0.15
-
D-fructose 6-phosphate
-
pH 8.2, 30C, cosubstrate CTP
0.16
-
D-fructose 6-phosphate
-
pH 8.5, 30C
0.18
-
D-fructose 6-phosphate
-
pH 8.4
0.19
0.2
D-fructose 6-phosphate
-
-
0.19
0.2
D-fructose 6-phosphate
-
-
0.2
-
D-fructose 6-phosphate
-
pH 8.5, 30C, D127S mutant PFK
0.24
-
D-fructose 6-phosphate
-
-
0.25
-
D-fructose 6-phosphate
-
pH 7.5
0.29
-
D-fructose 6-phosphate
-
pH 7.15, 25C, in the presence of 0.1 mM fructose 2,6-bisphosphate
0.3
-
D-fructose 6-phosphate
-
pH 8.0, 25, at a Mg2+/ATP ratio of 2/1
0.37
-
D-fructose 6-phosphate
-
pH 7.15, 25C, in the presence of 1 mM AMP
0.44
-
D-fructose 6-phosphate
-
pH 7.8, 50C
0.45
-
D-fructose 6-phosphate
-
pH 8.0, 25C, erythrocyte PFK
0.5
-
D-fructose 6-phosphate
-
pH 7.9, 24C
0.57
-
D-fructose 6-phosphate
-
pH 6.0, 50C
0.6
-
D-fructose 6-phosphate
-
pH 8.0, 25, at a Mg2+/ATP ratio of 1.4/1
0.62
-
D-fructose 6-phosphate
-
pH 8.0, 25C
0.68
-
D-fructose 6-phosphate
-, Q9YG89
pH 6.7, 85C
0.71
-
D-fructose 6-phosphate
-
-
1.17
-
D-fructose 6-phosphate
-
pH 6.0, 85C
1.212
-
D-fructose 6-phosphate
Q9YG89
pH 6.5, 95C, discontinuous assay
1.4
-
D-fructose 6-phosphate
-
pH 8.0, 25, at a Mg2+/ATP ratio of 0.7/1
1.43
-
D-fructose 6-phosphate
-
pH 7.9
1.44
-
D-fructose 6-phosphate
-
pH 7.0, 25C
1.5
-
D-fructose 6-phosphate
-
-
1.58
-
D-fructose 6-phosphate
-
pH 7.15, 25C
1.7
-
D-fructose 6-phosphate
A1XM06, A1XM07, -
30C, pH 7.8; 30C, pH 7.8
1.8
-
D-fructose 6-phosphate
-
pH 8.0, phosphorylated PFK
2.15
-
D-fructose 6-phosphate
-
pH 7.0, 37C
3.44
-
D-fructose 6-phosphate
-
pH 7.0, 50C
7
-
D-fructose 6-phosphate
-
pH 8.0, native PFK
254
-
D-fructose 6-phosphate
-
pH 8.5, 30C, R252Q mutant PFK
0.6
-
D-glucose 6-phosphate
-, Q9YG89
pH 6.7, 85C
5
-
D-ribose
-, Q9YG89
pH 6.7, 85C
3
-
D-ribose 5-phosphate
-, Q9YG89
pH 6.7, 85C
1
-
fructose
-, Q9YG89
pH 6.7, 85C
0.01
-
fructose 6-phosphate
-
12 h after isoproterenol administration
0.016
-
fructose 6-phosphate
-
pH 7.0, 25C, cytosolic PFK
0.039
-
fructose 6-phosphate
-
pH 8.0, 30C
0.2
-
fructose 6-phosphate
-
pH 7.7
0.0006
-
GTP
-
pH 7.2, 25C, cytosolic PFK
0.0009
-
GTP
-
pH 8.0, 25C, cytosolic PFK
0.008
-
GTP
-
pH 7.2, 25C, plastid PFK
0.013
-
GTP
-
pH 8.0, 25C, plastid PFK
0.038
-
GTP
-
pH 7.3, 25C, PFK II
0.08
-
GTP
-
pH 7.8, 30C
1.36
-
GTP
-
pH 7.8, 50C
4.3
-
GTP
-
pH 7.2, 30C
0.003
-
ITP
-
pH 8.0, 25C, pH 7.2, 25C, cytosolic PFK
0.004
-
ITP
-
pH 7.2, 25C, plastid PFK
0.011
-
ITP
-
pH 8.0, 25C, plastid PFK
0.035
-
ITP
-
pH 7.3, 25C, PFK II
0.082
-
ITP
-
pH 8.0, 25C, PFK I
2.2
-
ITP
-
pH 7.2, 30C
20
-
K+
-
pH 8.0, 28C
0.01
-
Mg2+
-
pH 7.9, 24C
0.025
-
Mg2+
-, Q8VU09
pH 7.5, 37C
0.18
-
NH4+
-
pH 8.0, 28C
0.009
-
UTP
-
pH 7.2, 25C, cytosolic PFK
0.01
-
UTP
-
pH 8.0, 25C, plastid PFK
0.018
-
UTP
-
pH 8.0, 25C, cytosolic PFK
0.019
-
UTP
-
pH 7.2, 25C, plastid PFK
0.032
-
UTP
-
pH 7.3, 25C, PFK II
0.055
-
UTP
-
pH 8.0, 25C, PFK I
5.1
-
UTP
-
pH 7.2, 30C
0.18
-
MgATP2-
-
; pH 7.5
additional information
-
additional information
-
cooperativity with respect to fructose 6-phosphate
-
additional information
-
additional information
-
kinetic mechanism
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic study; oligomeric form exhibits negative cooperativity with fructose 6-phosphate
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
pH-dependence of kinetic properties of cytosolic and plastid isozymes
-
additional information
-
additional information
Dunaliella marina
-
kinetic study
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic properties of phosphorylated enzyme; kinetic study
-
additional information
-
additional information
-
kinetic properties of phosphorylated enzyme; kinetic study
-
additional information
-
additional information
-
allosteric kinetics at alkaline pH-values; kinetic properties of phosphorylated enzyme; kinetic study
-
additional information
-
additional information
-
kinetic properties of phosphorylated enzyme; kinetic study
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
pH-dependence of kinetic properties of cytosolic and plastid isozymes
-
additional information
-
additional information
-
effects of low temperature and anoxia on kinetic constants
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
kinetic properties of dansylated enzyme
-
additional information
-
additional information
-
kinetic study
-
additional information
-
additional information
-
pH-dependence of kinetic properties of cytosolic and plastid isozymes
-
additional information
-
additional information
-
effects of temperature on kinetic properties
-
additional information
-
additional information
-
kinetic model of phosphofructokinase-1
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.037
-
ATP
-
wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.24
-
ATP
-
mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
9
-
ATP
-
mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
62
-
ATP
-
wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
236
-
ATP
-
wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25C
357
-
ATP
-
wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25C
0.016
-
D-fructose 6-phosphate
-
pH 7.2, 30C, cosubstrate gamma-thio-ATP
44
-
D-fructose 6-phosphate
P06999
in the presence of 0.5 mM MgATP2-, at pH 8.2 and 25C
60
-
D-fructose 6-phosphate
P06999
in the presence of 0.1 mM MgATP2-, at pH 8.2 and 25C
3.2
-
fructose 1,6-bisphosphate
-
reverse raction, recombinant enzyme
0.015
-
fructose 6-phosphate
-
pH 8.0, 8.5C, T125A mutant PFK
0.3
-
fructose 6-phosphate
-
pH 8.5, 30C, R72H mutant PFK
0.303
-
fructose 6-phosphate
-
pH 8.0, 8.5C, R72E mutant PFK
3.47
-
fructose 6-phosphate
-
pH 8.0, 8.5C, R171E mutant PFK
3.7
-
fructose 6-phosphate
-
pH 8.5, 30C, R252Q mutant PFK
5
-
fructose 6-phosphate
-
pH 8.2, 5C
49
-
fructose 6-phosphate
-
pH 7.2, 30C, cosubstrate ATP
57.2
-
fructose 6-phosphate
-
pH 8.5, 30C, I126A mutant PFK
60
-
fructose 6-phosphate
-
pH 8.2, 15C
61
-
fructose 6-phosphate
-
pH 8.0, 8.5C, wild-type PFK
88
-
fructose 6-phosphate
-
pH 7.2, 30C, at 2mM ATP
110
-
fructose 6-phosphate
-
pH 8.2, 25C
111
-
fructose 6-phosphate
-
pH 8.5, 30C, wild-type PFK
112
-
fructose 6-phosphate
-
forward reaction, recombinant enzyme
126
-
fructose 6-phosphate
-
pH 8.2, 30C, G212V mutant PFK
149
-
fructose 6-phosphate
-
pH 8.2, 30C, native PFK
167
-
fructose 6-phosphate
-
pH 8.5, 30C
185
-
fructose 6-phosphate
-
pH 8.2, 37C
additional information
-
additional information
-
kcat increases with pH, addition of GDP increases Kcat at constant pH
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2
-
ATP
-
mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
4
180
-
ATP
-
mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
4
5200
-
ATP
-
wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
4
7000
-
ATP
-
wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
4
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.9
-
2-oxoglutarate
-
pH 7.5
0.0207
-
3-phosphoglycerate
-
Ki(slope)
0.0679
-
3-phosphoglycerate
-
Ki(intercept)
2.1
-
3-phosphoglycerate
-
pH 7.9
1.3
-
ADP
-
mutant enzyme N341A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
1.6
-
ADP
-
mutant enzyme S377A/K678A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
1.75
-
ADP
-
pH 7.9
2
-
ADP
-
mutant enzyme K678A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
2.1
-
ADP
-
wild type enzyme, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
2.3
-
ADP
-
mutant enzyme N341A/R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
2.4
-
ADP
-
mutant enzyme S377A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
2.5
-
ADP
-
mutant enzyme R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
3.2
-
ADP
-
mutant enzyme H242A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; mutant enzyme K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
3.4
-
ADP
-
mutant enzyme R246A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
2.5
-
alpha-ketoglutarate
-
brain PFK
0.05
-
ammonium sulfate
-, Q9YG89
pH 6.7, 85C
0.25
-
ATP
-
pH 7.0
0.5
-
ATP
-
pH 8.0, native PFK
0.7
-
ATP
-
mutant enzyme D543A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.8
-
ATP
-
pH 6.8, 30C
0.9
-
ATP
-
mutant enzyme D543A, in the presence of 0.1 mM 2'-iodo-ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
1.1
-
ATP
-
mutant enzyme D543A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
1.4
-
ATP
-
pH 8.0, phosphorylated PFK
1.4
-
ATP
-
mutant enzyme D543A, in the presence of 0.1 mM 5-phospho-alpha-D ribose 1-diphosphate, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; mutant enzyme N341A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
1.4
-
ATP
-
mutant enzyme N341A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
1.6
-
ATP
-
mutant enzyme S377A/K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
1.9
-
ATP
-
mutant enzyme K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
2
-
ATP
-
wild type enzyme, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
2.1
-
ATP
-
mutant enzyme N341A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
2.2
-
ATP
-
mutant enzyme S377A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
2.3
-
ATP
-
mutant enzyme D543A, in the presence of 1 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; mutant enzyme D543A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
3
-
ATP
-
wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25C
3.1
-
ATP
-
mutant enzyme S377A/K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
4.3
-
ATP
-
mutant enzyme K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
5.2
-
ATP
-
mutant enzyme N341A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
5.2
-
ATP
-
mutant enzyme N341A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; mutant enzyme S377A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
5.3
-
ATP
-
wild type enzyme, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
5.6
-
ATP
-
mutant enzyme K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
5.8
-
ATP
-
mutant enzyme S377A/K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
5.9
-
ATP
-
mutant enzyme N341A/R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
6.8
-
ATP
-
mutant enzyme H242A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
7.6
-
ATP
-
mutant enzyme N341A/R246A/K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
8.1
-
ATP
-
mutant enzyme K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
8.5
-
ATP
-
wild type enzyme, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
8.6
-
ATP
-
mutant enzyme R246A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; mutant enzyme S377A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
8.8
-
ATP
-
mutant enzyme N341A/R246A/K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
9.5
-
ATP
-
mutant enzyme K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
10
-
ATP
-
Ki above 10 mM, mutant enzyme H242A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; Ki above 10 mM, mutant enzyme H242A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; Ki above 10 mM, mutant enzyme K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; Ki above 10 mM, mutant enzyme R246A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; Ki above 10 mM, mutant enzyme R246A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; Ki above 10 mM, mutant enzyme R246A/K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; Ki above 10 mM, mutant enzyme R246A/K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C; Ki above 10 mM, mutant enzyme R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25C
0.2
-
Ca2+
-
pH 6.8, 30C
0.1
-
cis-aconitate
-
brain PFK
0.03
-
citrate
-
brain PFK
0.25
-
citrate
-
pH 7.8, 30C, at 0.1 mM ATP
0.4
-
citrate
-
pH 7.8, 30C, at 0.5 mM ATP
1.3
-
citrate
-
pH 7.5, theoretical value
1.5
-
citrate
-
pH 7.8, in presence of 5 mM Mg2+, native enzyme form
2.4
-
citrate
-
pH 7.9
0.41
-
diphosphate
-
pH 7.7, 25C
0.2
-
Isocitrate
-
brain PFK
3.57
-
Isocitrate
-
pH 7.5
0.1
-
KCl
-, Q9YG89
pH 6.7, 85C
0.6
-
malate
-
brain PFK
1.43
-
malate
-
pH 7.5
1
-
NaCl
-, Q9YG89
pH 6.7, 85C
0.0272
-
phosphoenolpyruvate
-
Ki(slope)
0.15
-
phosphoenolpyruvate
-
pH 7.8, 30C
0.187
-
phosphoenolpyruvate
-
Ki(intercept)
0.8
-
phosphoenolpyruvate
-
pH 7.9
0.83
-
phosphoenolpyruvate
-
pH 7.2, 25C, mammary gland and ascites tumor PFK
1.5
-
succinate
-
brain PFK
3.21
-
succinate
-
pH 7.5
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0015
-
palmitoyl-CoA
-
in 50 mM imidazole, pH 8.0, containing 50 mM KCl and 2 mM MgCl2, at 22C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0056
-
-
pH 6.0, 37C, activity in undialyzed cell extracts
0.04
-
-
crude extract
0.38
-
Dunaliella marina
-
-
3.6
-
-
PFK III
5.5
-
-
PFK II
6
-
-
PFK I
15
-
-
cytosolic PFK
20.5
-
-
cytosolic PFK
21
-
-
plastid PFK
27
-
-
plastid PFK
48
-
-
leucoplast PFK
49.6
-
-
-
50
-
-
liver PFK
62
-
-
at 50C
65
-
-
euthermic animal
67.5
-
-
-
70
-
-
pH 7.2, 22C
76
-
-
hibernating animal
90
-
-
-
93
-
-
heart muscle PFK
95
-
-
brain PFK
99.5
-
-
human skeletal muscle
100
-
-
liver PFK
106.3
-
-
muscle PFK
120
160
-
skeletal muscle PFK
128
-
-
kidney PFK
136
-
Q9WUA3
recombinant C-type PFK
139
-
-
erythrocyte enzyme
150
-
-
heart PFK
160
-
-
heart PFK
160
-
-
muscle PFK
190
-
-
isoenzyme PFK1
200
-
-
isoforms I-IV
205
-
-
isoenzyme PFK2
206
-
-
liver PFK
265
-
-
muscle PFK
600
-
A1XM06, A1XM07, -
-
627
-
-
after 15700fold purification
2077
-
-
-
additional information
-
-
PFK activity is probably coregulated by binding of PFK to myofibrils
additional information
-
-
specific activity increases with increasing amounts of PFK, approx. 50% of maximal spec. activity at approx. 0.001 mg/ml, maximal activity at approx. 0.0035 mg/ml
additional information
-
-
slight increase in rats 12 h after isoproterenol administration
additional information
-
O08333, Q9FC99, Q9L1L8, -
characterization of the PFKA2-deletion strain by metabolic flux analysis and transcription analysis, transcriptional changes in regulatory and membrane proteins as well as in fatty acid metabolism, carbon flux through the pentose phosphate pathway increased, PFKA2 protein involved in determining the carbon flux distribution, production of the pigmented antibiotics actinorhodin and undecylprodigiosin up to 6fold increased in the deletion strain; integrated analysis of gene expression data by genome-scale metabolic model simulations, deletion mutant strain produces antibiotics in quantities comparable with that of the reference strain, enzyme activities like in wild-type attributed to intact copy of pfkA2 gene; integrated analysis of gene expression data by genome-scale metabolic model simulations, deletion mutant strain produces antibiotics in quantities comparable with that of the reference strain, wild type-like phosphofructokinase activities measured, attributed to intact copy of pfkA2 gene
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
6.5
Q9YG89
-
6.2
-
-
R72H mutant PFK, strong decrease in activiy above
6.5
-
-
isoenzyme PFK2, pH-optima at pH 6.5 and pH 8.5
6.7
8.3
-
endosperm
6.7
8.3
-
cytosolic isozyme
6.7
-
-, Q9YG89
-
6.7
-
-
forward direction, at 75C, 50% of maximal activity at pH 5.7, 80% at pH 7.7
7
-
Dunaliella marina
-
-
7
-
-
native enzyme
7
-
-
optimum depends on the ATP and fructose 6-phosphate concentration
7.1
-
-
ATP-independent, K+ or SO42- slightly shift to alkaline
7.2
8
-
fructose 6-phosphate phosphorylation
7.2
-
-
80% of maximal activity at pH 6.6
7.3
8.7
-
solubilized enzyme
7.3
-
-
PFK II
7.5
8.5
-
membrane-bound enzyme
7.6
8
-
plastid isoenzyme
7.6
-
-
ITP, optima at pH 7.6 and pH 8.2
7.6
-
-
phosphorylated enzyme
7.8
-
-
with ATP
7.8
-
-
optimum is shifted to approx. pH 7.5 in the presence of polyethylene glycol
8
8.25
-
-
8
8.5
-
AMP, fructose 2,6-bisphosphate, and phosphate lower the pH optimum to approx. pH 7.6, 7.8 and 7.6, respectively
8
-
-
plastid isoenzyme
8
-
-
small intestine PFK, 85-90% of maximal activity at pH 7.0
8
-
-
PFK I
8
-
-
above pH 8, PFK lost all its regulatory properties and showed maximum activity; above pH 8, the enzyme loses all its regulatory properties and shows maximal activity
8.2
-
-
ITP, optima at pH 7.6 and pH 8.2
8.5
9
-
cytosolic isoenzyme from leaf
8.5
-
-
isoenzyme PFK2, pH-optima at pH 6.5 and pH 8.5
additional information
-
-
-
additional information
-
-
pH-optimum depends on nucleoside triphosphate substrate
additional information
-
-
pH-dependence is influenced by Mg2+ and/or phosphate
additional information
-
-
pH-dependence of kinetic properties
additional information
-
-
pH-dependence of kinetic properties
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
6
-
30% of maximal activity at pH 4.5, 80% at pH 6.0
5
10.5
-
approx. 10% of maximal activity at pH 5.5, approx. 50% at pH 7.0
5
8.5
-, Q9YG89
60% of maximal activity at pH 5.0 and pH 8.5
5.5
6.5
-
about 50% of maximal activity at pH 5.5, about 25% of maximal activity at pH 6.5
5.5
7.5
Q9YG89
the pH optimum for activity of the enzyme is analysed only between the pH values of 5.5 to 7.5 due to concerns about instability of the ATP at more acid pH values and is found to be maximal between 5.5 and 6.5, but possesses 69% of maximal activity at pH 7.5
5.5
8.5
-
approx. 60% of maximal activity at pH 5.5, approx. 75% of maximal activity at pH 8.5
6
8.5
Dunaliella marina
-
approx. half-maximal activity at pH 6 and pH 8.5
6.3
8.7
-
PFK II, approx. 30% of maximal activity at pH 6.5, approx. 10% of maximal activity at pH 8.6
6.5
8.5
-
approx. half-maximal activity at pH 6.5 and pH 8.2
6.5
9
-
PFK I, approx. 10% of maximal activity at pH 6.5, approx. 60% of maximal activity at pH 9.0
6.8
9
-
approx. half-maximal activity at pH 6.8 and 9, plastid isoenzyme
7
8
-
approx. 60% of maximal activity at pH 7, approx 95% of maximal activity at pH 8
7
8.5
-
less than 5% of maximal activity at pH 7.0, approx. 50% of maximal activity at pH 7.5, pH curve is shifted to the left in the presence of 10% polyethylene glycol
7
9
-
approx. 80% of maximal activity at pH 7 and pH 9, approx. half-maximal activity at pH 6.7
7
9.3
-
approx. half-maximal activity at pH 7.0, approx. 70% or 80% of maximal activity at pH 9.3, membrane-bound or solubilized enzyme, respectively
7.4
8.5
-
approx. half-maximal activity at pH 7.4, maximal activity at pH 8.5, activators shift the optimum to lower pH-values
7.5
8.3
-
approx. half-maximal activity at pH 7.5, maximal activity at pH 8.3, approx. 15% of maximal activity at pH 7
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
assay at
20
-
-
assay at
22
-
-
assay at
24
-
-
assay at
24
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
26
-
-
assay at
27
28
-
assay at
27
28
-
assay at
27
28
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
37
-
-
assay at
90
-
-, Q9YG89
-
95
-
Q9YG89
assay at
additional information
-
-
effects of temperature on kinetic properties
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
100
-
very low activity at 20C, exponential increase in activity between 40C and 93C, approx. 50% of maximal activity at 80C, activation energy: 54 kJ/mol
40
100
-
very low activity at 40C, approx. 50% of maximal activity at 70C, activation energy: 42kJ/mol
40
100
-, Q9YG89
very low activity at 40C and 100C, approx. 50% of maximal activity at 75C, activation energy: 57 kJ/mol
85
95
Q9YG89
85C: 50% of maximal activity, 95C: optimum
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
isoelectric focusing
6
-
-
chromatofocusing
7.1
-
-
isoelectric focusing
7.4
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
low expression
Manually annotated by BRENDA team
-
M-type, i.e. muscle-type, C-type, i.e. fibroplast-type, and L-type, i.e. liver-type, PFK isoforms
Manually annotated by BRENDA team
-
strong expression of PFK-L
Manually annotated by BRENDA team
-
L- and C-type PFK isoenzymes, to a lesser amount M-type PFK
Manually annotated by BRENDA team
-
insulin induces a detachment of the enzyme from the erythrocyte membrane, thereby activating the enzyme
Manually annotated by BRENDA team
-
insulin may increase the glucose consumption in human erythrocytes, through a mechanism involving Ca2+ influx, calmodulin and the detachment of 6-phosphofructose-1-kinase from the erythrocyte membrane
Manually annotated by BRENDA team
-
ripened fruit
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
polymorphonuclear leukocytes, predominance of L-type PFK
Manually annotated by BRENDA team
-
mRNA detected at very low level
Manually annotated by BRENDA team
-
lactating mammary gland
Manually annotated by BRENDA team
Aspergillus niger B60
-
-
-
Manually annotated by BRENDA team
-
INS-1 cells, M-type, i.e. muscle-type, C-type, i.e. fibroplast-type, and perhaps lesser amounts of L-type, i.e. liver-type, PFK isoforms
Manually annotated by BRENDA team
-
M-type, i.e. muscle-type, C-type, i.e. fibroplast-type, and perhaps lesser amounts of L-type, i.e. liver-type, PFK isoforms
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
-
germinating, dry
Manually annotated by BRENDA team
-
white skeletal muscle
Manually annotated by BRENDA team
-
only M-type, i.e. muscle-type PFK isoenzyme
Manually annotated by BRENDA team
-
strong expression of PFK-L. Two types of phosphofructokinase-1 (PFK-L and PFK-M) differentially regulate the glycolytic pathway in insulin-stimulated chicken skeletal muscle, two types of phosphofructokinase-1 (PFK-L and PFK-M) differentially regulate the glycolytic pathway in insulin-stimulated chicken skeletal muscle
Manually annotated by BRENDA team
-
PFKMS is anchored in the principal piece of the sperm flagellum
Manually annotated by BRENDA team
-
localized in the mid-piece and principal piece of the flagellum as well as in the acrosomal area at the top of the head and in the cytoplasmic droplets released from the mid-piece after ejaculation, PFK shows no tight binding to sperm structures. It can readily be extracted from ejaculated boar spermatozoa by sonication. PFK is localized in the mid-piece and principal piece of the flagellum as well as in the acrosomal area at the top of the head and in the cytoplasmic droplets released from the mid-piece after ejaculation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Dunaliella marina
-
exclusively
Manually annotated by BRENDA team
-
possibly located in chloroplast
Manually annotated by BRENDA team
-
cytosolic and plastidic isoenzyme
Manually annotated by BRENDA team
-
cytosolic and plastidic isoenzyme
Manually annotated by BRENDA team
-
cytosolic and plastidic isoenzyme
Manually annotated by BRENDA team
Dunaliella marina
-
chloroplasts
Manually annotated by BRENDA team
additional information
-
subcellular distribution
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
29000
-
Q9YG89
gel filtration
35000
-
-
gel filtration at pH 8
63000
-
-
gel filtration
85000
-
P78985
native enzyme, gel filtration
90000
-
-
gel filtration
110000
-
-, Q8VU09
gel filtration
115000
-
-, Q9YG89
gel filtration
135000
-
-
sucrose density gradient centrifugation
135000
-
-
-
140000
-
-
gel filtration
140000
-
-
gel filtration
141000
142000
-
-
144000
-
-
high speed sedimentation equilibrium analysis
144500
-
-
gel filtration
160000
-
-
PFK II, gel filtration
175000
-
-
plastid PFK, gel filtration
180000
-
-
-
180000
-
-
major form, gel filtration at pH 7.5 or 8.0
182000
-
-
-
196000
-
-
isoform I, gel filtration
200000
-
-
recombinant PFK, gel filtration
200000
-
A1XM06, A1XM07, -
gel filtration; gel filtration; gel filtration
200000
-
-
gel filtration
201000
-
-
isoform II, gel filtration
203000
-
-
isoform III, gel filtration
210000
-
-
gel filtration
210000
-
-
PFK I, gel filtration
220000
-
-
leukoplast PFK, gel filtration
220000
-
-
glycerol density gradient centrifugation
280000
-
-
gel filtration, smallest catalytically active form, tends to aggregate to different active forms
282000
-
Dunaliella marina
-
30 h sucrose density gradient centrifugation
300000
-
-
gel filtration
300000
-
-
solubilized enzyme, gel filtration
300000
-
-
gel filtration
320000
-
-
-
330000
-
-
-
335000
-
-
-
360000
-
-
-
360000
-
-
gel filtration at high ionic strength, in 50 mM Tris-phosphate buffer plus 5 mM dithiothreitol, the enzyme aggregates to higher molecular weight form of 520000 Da
360000
-
-
glycerol density gradient centrifugation
380000
-
-
skeletal muscle
380000
-
-
-
380000
-
-
gel filtration
398000
-
-
gel filtration at high ionic strength, in 50 mM Tris-phosphate buffer plus 5 mM dithiothreitol, the enzyme aggregates to higher molecular weight forms of 520000 Da and 660000 Da
400000
-
-
gel filtration
400000
-
-
-
413000
-
-
native PAGE
434000
-
Dunaliella marina
-
15 h sucrose density gradient centrifugation
478000
-
-
gel filtration
500000
-
-
erythrocyte, sucrose density gradient centrifugation
510000
-
-
native enzyme, gel filtration
644000
-
Dunaliella marina
-
5 h sucrose density gradient centrifugation
662000
-
-
gel filtration
790000
-
-
sedimentation equilibrium
800000
-
-
isoform IV, gel filtration
835000
-
-
sedimentation equilibrium analysis
845000
-
-
sedimentation equilibrium analysis
975000
-
-
sedimentation equilibrium analysis
3500000
-
-
above, sedimentation velocity studies, concentration dependent molecular weight
6000000
-
-
gel filtration, largest catalytically active form, tends to aggregate to different active forms
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 76000, SDS-PAGE
?
-
x * 113000 + x * 98000 + x * 34000, 34000 Da non-covalently complexed protein component seems to be necessary for activity, SDS-PAGE
?
-
x * 78700, L-type PFK, immunoblot
?
-, Q8VU09
x * 48500, deduced from nucleotide sequence
?
-
x * 86200, M-type PFK, immunoblot
?
P90521
x * 92400, deduced from nucleotide sequence
?
-
x * 36500, sedimentation equilibrium centrifugation in 6 M guanidine
?
-
x * 119000 + x * 102000, encoded by KLPFK1 and KLPFK2 genes, SDS-PAGE
?
-
x * 74250, L-type PFK
?
-
x * 87500, c-type PFK, immunoblot
?
-
x + 82000, C-type PFK, x * 79500, M-type PFK
?
-, Q8VYN6, Q94AA4, Q9C5J7, Q9FIK0, Q9FKG3, Q9M076, Q9M0F9
x * 49200, calculated from sequence
?
-, Q8VYN6, Q94AA4, Q9C5J7, Q9FIK0, Q9FKG3, Q9M076, Q9M0F9
x * 50800, calculated from sequence
?
-, Q8VYN6, Q94AA4, Q9C5J7, Q9FIK0, Q9FKG3, Q9M076, Q9M0F9
x * 52000, calculated from sequence
?
-, Q8VYN6, Q94AA4, Q9C5J7, Q9FIK0, Q9FKG3, Q9M076, Q9M0F9
x * 53500, calculated from sequence
?
-, Q8VYN6, Q94AA4, Q9C5J7, Q9FIK0, Q9FKG3, Q9M076, Q9M0F9
x * 53600, calculated from sequence
?
-, Q8VYN6, Q94AA4, Q9C5J7, Q9FIK0, Q9FKG3, Q9M076, Q9M0F9
x * 58500, calculated from sequence
?
-, Q8VYN6, Q94AA4, Q9C5J7, Q9FIK0, Q9FKG3, Q9M076, Q9M0F9
x * 58600, calculated from sequence
dimer
-, Q8VU09
2 * 50000, SDS-PAGE
dimer
-
2 * 37000, isoenzyme PFK2, SDS-PAGE
dimer
-
calmodulin-bound dimers are active and less susceptible to inhibition by allosteric ligands, 5 mM ATP stabilizes phosphofructokinase dimers
heterooctamer
P16862
x-ray crystallography
heterooctamer
Saccharomyces cerevisiae PS1
-
x-ray crystallography
-
heterotetramer
P00511
x-ray crystallography
hexamer
-
6 * 67000, muscle enzyme, sedimentation equilibrium ultracentrifugation or gel filtration in 6.5 M guanidine
hexamer
-
6 * 76500, SDS-PAGE
homodimer
-
2 * 100000, gel filtration
homohexamer
-
6 * 86000, apparent molecular weight estimated from SDS-PAGE
homotetramer
P00512
x-ray crystallography
homotetramer
P06999
x-ray crystallography
monomer
Q9YG89
1 * 29000, SDS-PAGE
octamer
-
alpha2beta4alpha2 or beta2alpha4beta2, 4 * 118000 + 4 * 112000, SDS-PAGE
octamer
-
8 * 103306, MALDI-TOF mass spectrometry
octamer
-
x * 98000 + x * 108000, SDS-PAGE
octamer
-
8 * 81000, SDS-PAGE
octamer
-
electron microscopy studies of Pfk1 to characterize the quaternary structure of the enzyme in the active and inhibited states. The molecule can be described as composed of two subdomains, connected by two well-defined densities
octamer
-
the structure of Pfk1 (beta2alpha4beta2) in the T-state (generated by incubating the enzyme with saturating amounts of Mg-ATP) is determined by cryo-electron microscopy
octamer
Schizosaccharomyces pombe CBS1057
-
8 * 103306, MALDI-TOF mass spectrometry
-
oligomer
-
x * 46300 + x * 49500 + x * 50000 + x * 53000, 4 enzyme forms of different subunit composition, SDS-PAGE with 4 M urea
oligomer
Escherichia coli DF1020
-
-
-
tetramer
-
-
tetramer
-
-
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
SDS-PAGE
tetramer
-
4 * 52000, SDS-PAGE
tetramer
-
4 * 49000, SDS-PAGE
tetramer
-
4 * 90000, SDS-PAGE
tetramer
-
4 * 80000
tetramer
-
alpha4, 4 * 33000, SDS-PAGE
tetramer
-
4 * 55585, recombinant PFK, MALDI-TOF mass spectrometry
tetramer
-, Q9YG89
alpha4, x * 33392, deduced from nucleotide sequence
tetramer
-
alpha4, 4 * 34447, deduced from nucleotide sequence
tetramer
-
4 * 82000, SDS-PAGE
tetramer
-
4 * 70000, SDS-PAGE, smallest catalytically active form
tetramer
-
alpha4, 4 * 34000, SDS-PAGE
tetramer
-
4 * 94600-95000, SDS-PAGE
tetramer
-
4 * 84500, SDS-PAGE
tetramer
-
4 * 57000, leukoplast PFK, SDS-PAGE
tetramer
-
x * 47200 + x * 42400 + x * 40400, plastid isozyme
tetramer
-
4 * 37000, isoenzyme PFK2, SDS-PAGE in the presence of 1 mM ATP, 5 mM Mg2+
tetramer
-
4 * 35000, high speed sedimentation equilibrium centrifugation or PAGE in the presence of 8 M urea or 7 M guanidine
tetramer
-
1 * 92000 + 1 * 88000 + 2 * 86000, SDS-PAGE and densitometric analysis
tetramer
-
4 * 35000, isoenzyme PFK1, tetrahedral arranged subunits, SDS-PAGE
tetramer
-
x * 53300 + x * 41500 + x * 39000, cytosolic isozyme
tetramer
-
binding of calmodulin to the high affinity site of 6-phosphofructo-1-kinase induces dimerization of the enzyme, but does not inhibit the catalytic activity. Dissociation of the enzyme tetramers induced by calmodulin occurs under very low concentrations of the Ca2+-binding protein and requires Ca2+
monomer
Aeropyrum pernix DSM 11879
-
1 * 29000, SDS-PAGE
-
additional information
-
in the absence of substrates PFK2 is a dimer, in the presence of high concentrations of ATP or ATP analogs, this dimer aggregates into a tetramer, aggregation is reversed by adddition of fructose 6-phosphate
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
purified PFK contains 7-9 covalently bound phosphate groups per tetramer
phosphoprotein
P78985
in Aspergillus niger cells spontaneous posttranslational modification of 6-phosphofructo-1-kinase occurs in a two step process. The native enzyme (85 kDa) is first cleaved to an inactive fragment (49 kDa) that regains its activity after phosphorylation of the protein, the shorter fragment exhibits changed kinetics, such as resistance to citrate inhibition
proteolytic modification
-
spontaneous posttranslational modification of PFK1 leads to significant changes in allosteric regulation of the enzyme activity
proteolytic modification
-
the 49000 Da fragment is formed from the 85000 Da native enzyme by posttranslational modification. The native 85000 Da enzyme is moderately inhibited by citrate, the 49000 Da shorter fragment of PFK1 proves to be completely resistant to inhibition by citrate
phosphoprotein
-
the enzyme is regulated by phosphorylation
side-chain modification
P90521
2 putative cAMP-dependent protein kinase phosphorylation sites at Ser 293 and Ser 559
side-chain modification
-
-
side-chain modification
-
in vitro phosphorylation with cAMP-dependent protein kinase, 0.1-0.2 mol phosphate/mol of protomer, phosphorylation increases activity of PFK and reduces sensitivity to ATP inhibition
phosphoprotein
-
insulin increases phosphorylation of human erythrocyte enzyme
side-chain modification
-
in vitro phosphorylation of PFK fragment containing a cAMP-dependent protein kinase consensus site
side-chain modification
-
4.2 mol phosphate/mol of enzyme in rats treated with 3 doses of isoproterenol, 3 mol phosphate/mol enzyme after dephosphorylation, presence of phosphate groups influences the kinetic properties of PFK-1
phosphoprotein
-
phosphorylation of PFKM may exert a major role during starvation in fish muscle
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
concentrated PFK solution is mixed with solutions containing fructose 6-phosphate, ADP and 2-methyl-2,4-pentanediol in a glass tube to a final concentration of 4 mg/ml PFK, 50% 2-methyl-2,4-pentanediol, 0.2 mM fructose 6-phosphate, 5 or 10 mM ATP, 100 mM Tris-HCl, pH 8.3, 5 mM MgCl2, 2.4 mM dithiothreitol, and 2.4 mM EDTA, crystal structure of PFK complexed with fructose 1,6-bisphosphate, ATP/Mg2+ and ADP/Mg2+ at 2.4 A resolution
-
crystals are obtained from solutions containing 10 mg/ml PFK, 14% polyethylene glycol 6000, 1-1.1 M NaCl, 50 mM Tris-HCl, pH 7.7-7.9, crystal structure of PFK in the absence of ligands at 2.4 A resolution
-
isozyme Pfk-2 in complex with D-fructose 6-phosphate, hanging drop vapor diffusion method, using 23% (w/v) PEG 4000, 100 mM sodium acetate, pH 4.75, and 200 mM ammonium acetate
P06999
hanging drop vapor diffusion method, using 0.2 M calcium acetate hydrate, 0.1 M sodium cacodylate trihydrate pH 6.5, and 18% (w/v) polyethylene glycol 8000, at 16C
P00512
4 mg/ml PFK in 25 mM sodium phosphate buffer pH 7.0, is dialyzed at 4C against 25 mM phosphate buffer, pH 7.0, containing 10 mM 2-mercaptoethanol, 1 mM MgSO4, 1 mM EDTA, 2 mM ATP, 2 mM FDP and 23% ammonium sulfate, crystals appear after 8-10 weeks
-
hanging drop vapor diffusion method, using 16% (w/v) PEG 400, 0.1 M MgSO4, and 0.1 M acetate buffer (pH 5.3)
P00511
hanging drop vapor diffusion method, using 6-10% (w/v) PEG 4000 and 0.2 mM sodium acetate in 0.1 M 4-morpholineethanesulfonic acid buffer (pH 6.0)
P16862
hanging-drop vapour-diffusion, well solution consists of 1.7-1.8 M sodium formate, 100 mM sodium acetate, pH 4.6-4.8, hanging drop contains 4-5 mg/ml protein, 20 mM TEA buffer, pH 8.0, PFK is crystallized in the absence and presence of reaction products and the active site inhibitor 2,5-anhydro-1-deoxy-1-(m-nitro-D-mannitol-6-disodiumphosphate) at 2.9-4.0 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
fructose 6-phosphate, ATP or NH4+ stabilizes at 4C
7
9.3
-
solubilized enzyme, stable for 5 min at 30C
7
-
-
enhanced inactivation below, fructose 1,6-diphosphate stabilizes
7.8
-
-
membrane-bound enzyme, stable for 1 h at 30C
8
-
-
relatively stable to inactivation by dilution, muscle enzyme
8
-
-
below, stability is greatly diminished
additional information
-
-
heart enzyme, mild acidic conditions lead to reversible dissociation and decrease of activity, ATP or fructose 1,6-bisphosphate protects
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
liver enzyme, 2 h, 80% loss of activity by dissociation of enzyme
0
-
-
rapid inactivation in the presence of Mg2+, phosphoenolpyruvate and ATP, incubation at 30C reverses activity, inactivation is probably due to dissociation of a dimer into monomers
8
-
-
liver enzyme, 2 h, 60% loss of activity by dissociation of enzyme
30
-
-
membrane-bound enzyme, stable at pH 7.8 for 1 h, solubilized enzyme, stable at pH 7.0-9.3 for 5 min
40
60
-
30 min, stable
50
-
-
complete inactivation after 2 h without stabilizing agent, no inactivation after 2 h incubation in the presence of 1 M trehalose, enzyme incubated in the presence of 37.5% (v/v) glycerol is not protected against incubation at 50C. Incubation for 45 min at 50C in the presence of 7.525% glycerol (v/v) results in a 2-4times lower activity compared to control
58
-
-
t1/2: 3 min
60
-
-
3 min, inactivation, enzyme prepared by ATP-Sepharose chromatography
60
-
-
complete inactivation of PFK III after approx. 30 sec, ATP stabilizes, 30% loss of activity after 6 min in the presence of 1 mM ATP
66
-
-
3 min, complete inactivation
70
-
-
less than 20% loss of activity after 2 h
75
-
-
complete inactivation after 2 min
75
-
-
complete inactivation after 4 min
75
-
-
30% loss of activity after 15 min
79
-
-
complete inactivation after 3 min
80
-
-, Q9YG89
no loss of activity after 2 h
80
-
-
less than 20% loss of activity after 2 h
85
-
-
t1/2: 3 min
90
-
-
complete inactivation after 3 min
90
-
-
half-life grater than 5 h in phosphate buffer
95
-
-
50% loss of activity after 10 min, addition of 5 mM ADP and 25 mM MgCl2 increases the stability by up to 10C
95
-
-, Q9YG89
complete loss of activity after 2 h
95
-
-
complete loss of activity after 1 h
95
-
Q9YG89
half-life: 30 min
100
-
-
5 min, 70% loss of activity, enzyme prepared by DEAE-cellulose chromatography in the absence of MgATP
100
-
-
approx. 70% loss of activity after 10 min in the absence of substrates
100
-
-, Q9YG89
complete loss of activity after 30 min, 10% and 45% loss of activity after 30 min in the presence of 1 M KCl and NaCl, respectively
100
-
-
complete loss of activity after 20 min, 40% loss of activity after 2 h in the presence of 1 M ammonium sulfate
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dilution reversibly decreases activity
-
unstable in buffers like imidazole-HCl, pH 6.6 or 6.8, or Tris-HCl, pH 8, 50 mM phosphate and 0.3 M KCl stabilize
-
dilution inactivates
-
fructose 6-phosphate stabilizes, not 1 mM ATP or 50% v/v glycerol
-
D-fructose 6-phosphate stabilizes, less effective is KCl or phosphoenolpyruvate, only slightly stabilized by ATP or ATP/Mg2+
-
dilution inactivates
-
D-fructose 6-phosphate stabilizes, less effective is KCl or phosphoenolpyruvate, only slightly stabilized by ATP or ATP/Mg2+
-
dilution inactivates
-
50 mM phosphate stabilizes at pH 6.6
-
polyethylene glycol stabilizes
-
very unstable upon purification, dithioerythritol, K+ or Mg2+ and phosphate partially stabilize
Dunaliella marina
-
unstable to vigorous sonication or lyophilization
-
glycerol and KCl or ATP stabilize
-
dilution inactivates
-
fructose 6-phosphate, ATP, ADP, citrate, KCl or ammonium sulfate does not stabilize
-
glycerol prevents inactivation of dilute cytosolic enzyme solution
-
glycerol stabilizes
-
(NH4)2SO4 prevents enzyme from dissociation at pH 6.4
-
at least 15 mM phosphate required to stabilize PFK during purification, presence of 10% glycerol helps to stabilize
-
largest molecular weight-form of purified enzyme is the most stable form
-
labile at all stages of purification, particularly at high dilutions or high salt concentrations, glycerol, fructose 6-phosphate and high enzyme concentrations stabilize
-
dilution inactivates
-
dilution reversibly decreases activity
-
freeze-drying inactivates, addition of Zn2+ plus trehalose, maltose, sucrose, galactose or glucose stabilizes, more than 80% of the initial activity is retained in the presence of 0.4 mM Zn2+ and 100 mM trehalose, no stabilization in the presence of glucose or galactose or any other divalent cation alone
-
fructose 6-phosphate, fructose 1,6-bisphosphate and ammonium sulfate stabilize dilute enzyme solutions
-
glycine, proline, hydroxyproline, trimethylamine N-oxide, glycerol or myo-inositol affords a high degree of cryoprotection
-
very stable in Tris-phosphate or glycylglycine-glycerol buffer, pH 8, at 10-20 mg protein per ml
-
10% glycerol, dithiothreitol and PMSF stabilize during purification
-
cytosolic enzyme extremely unstable upon purification, substrates, metabolites, ethylene glycol or SH-compounds do not stabilize
-
cytosolic enzymes are less stable than plastidic
-
fructose 6-phosphate, MgCl2 and ethylene glycol stabilize
-
leaf cytosolic isozyme rather unstable upon purification
-
dilution inactivates
-
dilution leads to enzyme dissociation
-
fructose 6-phosphate, ATP or ammonium sulfate stabilizes during dialysis and storage at pH 6-9
-
PMSF stabilizes during purification
-
glycerol and KCl or ATP stabilize
-
dithioerythritol stabilizes
-
MgATP2- or ATP and Mg2+ stabilize during purification
-
sensitive to freezing, complete inactivation after 24 h at -20C at pH 7.5
-
glycerol and KCl or ATP stabilize
-
ATP stabilizes
-
glycerol prevents inactivation of dilute cytosolic enzyme solution
-
NaF, EDTA and PMSF stabilize during purification
-
AMP, ADP, fructose 6-phosphate or antipain stabilizes during purification
-
concentration by ultrafiltration on Amicon PM-10 membrane results in appreciable loss of activity, concentration in collodium bags allows higher protein concentration to be obtained without loss of activity
-
dilution leads to enzyme dissociation
-
cold labile, fructose 1,6-bisphosphate stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 40% glycerol, 6 months, no loss of activity
-, Q8VU09
4C, in saturated ammonium sulfate solution, decrease of activity, dithiothreitol restores
-
4C, under N2, in 50 mM Tris-potassium phosphate buffer, pH 8, 1 mM EDTA, 1.4 mM ammonium sulfate, 1 mM ATP, 0.2 mM KCl, 10 mM dithiothreitol, at least 6 months
-
4C, under nitrogen, in 50 mM Tris-potassium phosphate buffer, pH 8, 1 mM EDTA, 1.4 M (NH4)2SO4, 1 mM ATP, 0.2 M KCl, 10 mM dithiothreitol, at least 6 months
-
-20C, in phosphate buffer, 50% glycerol, 0.3% loss of activity per day
-
-20C, in 50 mM phosphate buffer, pH 7.5, 1 year, no loss of activity
-
2C, crystalline, in 45% saturated ammonium sulfate, at least 2 months
-
4C, t1/2: 1.5-2 days, ATP and/or fructose 1,6-bisphosphate increase stability
-
-20C, 0.1 M Tris-HCl buffer, pH 8, 2 mM MgCl2, 1 mM EDTA, 14 mM 2-mercaptoethanol, 10% v/v glycerol, 20% loss of activity within 3 weeks
-
4C, 65% saturated ammonium sulfate-suspension, at least 2 months, no loss of PFK1 activity
-
4C, enhanced stability in ammonium sulfate suspension
-
-20C, in 100 mM Tris-HCl buffer, pH 7.4, 1 mM dithiothreitol, 50% glycerol, stable
-
-20C, purified enzyme with 10% glycerol (v/v), 2 weeks, no loss of activity
-
5C, 50 mM potassium phosphate buffer, pH 8, 1 mM EDTA, 1 mM AMP, 1 mM dithiothreitol, 2 mM fructose 6-phosphate, 30% loss of activity per month
-
4C, precipitated in 50 mM potassium phosphate, pH 7.0, 5 mM 2-mercaptoethanol, 1 mM EDTA, 0.5 mM PMSF, several weeks, no loss of activity
-
-12C, Tris-glycerol buffer, pH 7.5, 50% v/v glycerol, up to 6 months, 10-20% loss of activity
-
4C, less stable at pH 6 and 8 than at neutral pH-values
-
3C, in concentrated ammonium sulfate suspension, in the presence of ATP, at least 1 month, no loss of activity
-
-15C, 3 days, complete loss of activity
-
4C, 1 week, 47% loss of activity
-
-20C, 0.06 mg protein/ml, in 20 mM phosphate buffer, pH 7.5, 40% v/v glycerol, 1 month
-
-20C, more than 2 mg protein per ml, in 50 mM Tris-phosphate buffer, pH 8, 2 mM EDTA, 100 mM ammonium sulfate, 0.1 mM ATP, 0.5 mM dithiothreitol, several months
-
-20C, purified enzyme with 10% glycerol (v/v), 2 weeks, no loss of activity
-
4C, crystalline, 6 years
-
very stable in Tris-phosphate or glycylglycine-glycerol buffer, pH 8, at high protein concentrations
-
-80C, frozen with liquid nitrogen, several months, no loss of leukoplast PFK activity
-
4C, 70% loss of activity within 20 h, leaf cytosolic isozyme, 5 mM MgCl2 and 20% v/v ethylene glycol stabilizes
-
ATP, 1 mM, stabilizes during storage for longer periods
-
-15C, at least 4 weeks
-
0C, dilute enzyme solution in 5 mM imidazole-HCl buffer, pH 7, 1 mM D-fructose 6-phosphate, 5 mM 2-mercaptoethanol, 0.5 mM PMSF, 6 h, 20% loss of activity
-
4C, concentrated enzyme solution, 50 mM potassium phosphate buffer, pH 7, 1 mM EDTA, 5 mM 2-mercaptoethanol, 0.5 mM PMSF, 1 mM fructose 6-phosphate, several months
-
4C, fructose 6-phosphate, ATP or NH4+ stabilizes at pH-values from 6 to 9
-
room temperature, 20% loss of activity within 1 month
-
-20C, 0.1 M Tris-HCl buffer, pH 8, 2 mM MgCl2, 1 mM EDTA, 14 mM 2-mercaptoethanol, 10% v/v glycerol, 20% loss of activity within 3 weeks
-
-20C, inactivation within 24 h
-
0-4C, more stable in Tris than in phosphate buffer
-
enzyme extracts prepared at pH 8 are less stable to storage at 0-4C than extracts prepared at pH 7.5
-
-20C, 0.1 M Tris-HCl buffer, pH 8, 2 mM MgCl2, 1 mM EDTA, 14 mM 2-mercaptoethanol, 10% v/v glycerol, 20% loss of activity within 3 weeks
-
-20C, 50 mM Tricine-NaOH buffer, pH 7.9, 50% v/v glycerol, at least 2 months
-
more stable if kept under nitrogen or with dithiothreitol
-
4C, 40 mM potassium phosphate, pH 7.0, 10 mM beta-mercaptoethanol, 0.1 mM EDTA, 2% glycerol, 6 mM fructose 6-phosphate, quick loss of activity
-
-20C, concentrated enzyme solution in 50 mM Tris-HCl buffer, pH 7.8, 60% glycerol, 1 mM EDTA, 10 mM dithiothreitol, 13% loss of activity per month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant PFK, Bio-Scale Q5, gel filtration
-, Q9YG89
ammonium sulfate, Levafix blue, Resource Q, Phenyl-Sepharose
-, Q8VU09
ammonium sulfate, ethanol, DEAE-cellulose, Sephadex G-200
-
DEAE-cellulose, phosphocellulose, ammonium sulfate
-
ammonium sulfate, Blue-Sepharose, density gradient centrifugation
-
; Cibacron Blue F3GA affinity chromatography, ion-exchange, gel filtration
-
ammonium sulfate, Sepharose 4b, DEAE-Sephacel
-
CM-Sephadex, calcium phosphate gel, Sephadex G-100, DEAE-Sephadex, hydroxyapatite
-
heat treatment, isopropanol, ammonium sulfate, DEAE-cellulose, crystallization
-
polyethylene glycol, ATP-agarose, Sephacryl S-300
-
2 immunologically distinct isozymes
-
; ammonium sulfate, ethanol, DEAE-cellulose, Sephadex G-200
-
DEAE-Sepharose, ATP-agarose, Resource S
-
10% (w/v) PEG precipitation, DE52 column chromatography, Blue-Sepharose column chromatography, phosphocellulose column chromatography, and Superdex 200 gel filtration
-
ammonium sulfate, DEAE-cellulose, partial purification
Dunaliella marina
-
protamine sulfate, ammonium sulfate, Sephadex G-200, partial purification
-
ammonium sulfate, acetone, QAE-Sephadex, acid, QAE-Sephadex, hydroxyapatite
-
overexpressed PFK, DEAE-cellulose, Cibacron blue, hydroxyapatite
-
PFK1, Blue Dextran, heat denaturation, PFK2, Sepharose-Blue Dextran, hydroxyapatite, ammonium sulfate, Blue Dextran, heat denaturation
-
DEAE-cellulose, ammonium sulfate, AMP-agarose
-
heat, ammonium sulfate, DEAE-Sephadex A50, Sepharose 6B, high speed centrifugation
-
Mimetic Blue 1 column chromatography and Mono Q column chromatography
P00512
10% (w/v) PEG precipitation, DE52 column chromatography, Blue-Sepharose column chromatography, phosphocellulose column chromatography, and Superdex 200 gel filtration
-
batch DEAE-cellulose, ammonium sulfate, heat, DEAE-cellulose, Blue Dextran
-
Cibacron Blue F3GA-Sephadex G75 gel filtration, Resource Q column chromatography, and BioSep SEC-S4000 gel filtration
-
PEG 6000 precipitation, Resource Q column chromatography, and BioSep SEC-S4000 gel filtration
-
QAE-Sepharose, partially purified
-
polyethylene glycol, Cibacron blue F 3G, Sepharose 6B, Resource Q, BioSil SEC 400
-
pseudo-affinity dye-ligand chromatography on Procion Blue H-5R-Sepharose
-
ATP-Sepharose affinity chromatography
-
ammonium sulfate, DEAE-Sephadex, Sephadex G-200
-
recombinant C-type PFK, ATP-Sepharose
Q9WUA3
monomeric form PFK-III, ammonium sulfate, heat treatment, Sepharose 6B, DEAE-sephacel
-
PFK I and PFK II, butyl-Sepharose, DEAE-Fractogel, Superose 6
-
Ni-NTA column chromatography and Superdex 200 gel filtration
-
ammonium sulfate, ethanol, DEAE-cellulose, Sephadex G-200
-
Cellulose-P, hydroxyapatite, ATP-agarose
-
ammonium sulfate precipitation DEAE-Sephacel gel filtration and Bio-Gel filtration
-
Cibacron Blue 3GA gel filtration, DE-52 column chromatography and ATP-N6-agarose column chromatography
P00511
liver PFK, ammonium sulfate, DEAE-Sephadex, agarose chromatography
-
liver PFK, heat treatment, protamine sulfate, ammonium sulfate, Sephacryl S-400
-
muscle PFK, isopropanol, heat treatment, ammonium sulfate, crystalization
-
PEG 6000 precipitation, Resource Q column chromatography, and BioSep SEC-S4000 gel filtration
-
ammonium sulfate, phenyl-Sepharose
-
DEAE Sepharose, Affi-gel blue
-
heat treatment, ammonium sulfate, Cibacron blue F3GA, Sephacryl S-500
-
native enzyme can only be prepared in the presence of proteinase inhibitors
-
52C, ammonium sulfate, QAE-Sephadex, ultrafiltration
-
leukoplast PFK, acetone powder, DEAE-Sephacel, Mono Q, Phenyl-Sepharose
-
plastid PFK, acetone powder, DEAE-Sephacel, AMP-agarose, DEAE-Sepharose
-
acetone, protamine sulfate, Matrex-blue A, Sephacryl S-300, very rapid purification
-
ammonium sulfate, Cibacron Blue F3G-A, gel filtration, ion-exchange
-
PEG 6000 precipitation at 3.5% and 14% (w/v) and Cibacron Blue F3G-A Sephadex G 100 gel filtration
P16862
protamine sulfate, ammonium sulfate, acetone, ammonium sulfate, Bio-Gel, DEAE-cellulose, hydroxyapatite
-
polyethylene glycol 6000, F3G-A-Sephadex, Resource Q
-
Blue Sepharose, ATP-Sepharose
-
isoforms I-IV, DEAE-Sephacel, Red-agarose, ATP-agarose, Mono Q
-
12% PEG6000 precipitation, ATP agarose column chromatography, DEAE-Sepharose column chromatography, phosphocellulose column chromatography, and Blue-Sepharose column chromatography
-
cytosolic PFK, ammonium sulfate, DEAE-Sephacel, Blue Sepharose, ATP-agarose
-
inclusion of adenosine 5'-(beta,gamma-imido)triphosphate is conducive to enzyme activitiy during the purification
A1XM06, A1XM07, -
protamine sulfate, Cibacron blue Sepharose, DEAE-Sephadex
-
gel filtration; gel filtration; gel filtration