Information on EC 2.7.1.105 - 6-phosphofructo-2-kinase

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

EC NUMBER
COMMENTARY
2.7.1.105
-
RECOMMENDED NAME
GeneOntology No.
6-phosphofructo-2-kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
mechanism
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
kinetic mechanism
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
random mechanism
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
O81398
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46
Q9MB58
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
high 6-phosphofructo-2-kinase activity compared to the fructose 2,6-bisphosphatase
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
high 6-phosphofructo-2-kinase activity compared to the fructose 2,6-bisphosphatase
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
bifunctional enzyme comprises both 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase, EC 3.1.3.46, activities
-
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
bifunctional enzyme comprises both 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase, EC 3.1.3.46, activities, residues K51, T52, D128, and K172 are key catalytic residues for the 6-phosphofructo-2-kinase activity
Q52MQ5, Q6PY95
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
HBP1 and HBP2 both show a random order equilibrium bi bi mechanism, bifunctional enzyme comprises both 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase, EC 3.1.3.46, activities
Q16875
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
ordered bi bi mechanism, structural and functional roles of Cys-238 and Cys-295
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fructose 2,6-bisphosphate biosynthesis
-
-
Fructose and mannose metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:beta-D-fructose-6-phosphate 2-phosphotransferase
Not identical with EC 2.7.1.11 6-phosphofructokinase. The enzyme co-purifies with EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6-phosphofructo-2-kinase
-
-
6-phosphofructo-2-kinase
Q16875
-
6-phosphofructo-2-kinase
-
-
6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
-
-
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Q16875
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
P70265
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
bifunctional enzyme
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Q52MQ5
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3
A7UAK4, A7UAK5, A7UAK6
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3
A7UAK3
-
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase:glucokinase complex
-
-
6-phosphofructose 2-kinase
-
-
-
-
6PF2K/Fru-2,6-P2ase
Q16875
-
ATP:D-fructose-6-phosphate 2-phosphotransferase
-
-
-
-
fructose 6-phosphate 2-kinase
-
-
-
-
inducible 6-phosphofructo-2-kinase
Q7TS91
-
iPFK2
Q7TS91
-
kinase, 6-phosphofructo-2-(phosphorylating)
-
-
-
-
OsF2KP1
Q75IQ9
-
OsF2KP2
-
-
Pfk-2
-
-
Pfk-2
Q16875
-
Pfk-2
P70265
-
Pfk-2
Q9JJH5
-
Pfk-2
Q6PY95
-
PFK-2/FBPase
-
-
PFK-2/FBPase-2
Q52MQ5
-
PFKFB-3
A7UAK4, A7UAK5, A7UAK6
-
PFKFB-3
A7UAK3
-
PFKFB1
P07953
-
PFKFB1
-
-
PFKFB3
Q7TS91
-
PFKFB3
-
gene name of isoform
PFKFB4
-
gene name of isoform
phosphofructikinase-2
-
-
phosphofructokinase 2
-
-
-
-
phosphofructokinase-2
-
-
phosphofructokinase-2/fructose bisphosphatase-2
-
-
tPFK-2
-
isoform, product of Pfkfb4 gene
uPFK-2
-
isoform, product of Pfkfb3 gene
CAS REGISTRY NUMBER
COMMENTARY
78689-77-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Columbia
-
-
Manually annotated by BRENDA team
strains DF903 and DF905 (mutant)
-
-
Manually annotated by BRENDA team
Jerusalem artichoke
-
-
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4
SwissProt
Manually annotated by BRENDA team
exon 15a and complete sequence; 10 splicing variants
SwissProt
Manually annotated by BRENDA team
human enzyme is 95% identical with rat or bovine enzyme
-
-
Manually annotated by BRENDA team
Pfkfb3 gene; overexpression of the Pfkfb3 gene in Mus musculus, generation of uPFK-2 transgenic line
SwissProt
Manually annotated by BRENDA team
recombinant
SwissProt
Manually annotated by BRENDA team
splice variant 1
SwissProt
Manually annotated by BRENDA team
splice variant 2
SwissProt
Manually annotated by BRENDA team
splice variant 3
A7UAK6
SwissProt
Manually annotated by BRENDA team
transgenic, kinase-active liver PKF-2, FVB background
SwissProt
Manually annotated by BRENDA team
marine mussle
-
-
Manually annotated by BRENDA team
crayfish
-
-
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
SwissProt
Manually annotated by BRENDA team
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
Manually annotated by BRENDA team
foetal and adult
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
male, Wistar background, primary culture of hepatocytes
SwissProt
Manually annotated by BRENDA team
splice variant
SwissProt
Manually annotated by BRENDA team
Sprague-Dawley rat
-
-
Manually annotated by BRENDA team
Zucker fa/fa rats
-
-
Manually annotated by BRENDA team
castor bean
-
-
Manually annotated by BRENDA team
baker's yeast, haploid strain X2180
-
-
Manually annotated by BRENDA team
potato plant, enzyme of Solanum tuberosum is 83% identical with enzyme of Zea mays and 72% identical with enzyme of Pinus taeda
SwissProt
Manually annotated by BRENDA team
teleost fish
-
-
Manually annotated by BRENDA team
stock 427
SwissProt
Manually annotated by BRENDA team
stock 427, bifunctional enzyme, 4 isozymes
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
PFKFB3 enzymes are activated in human cancers
metabolism
-
glycolytic enzyme is present as testis-specific isoforms, these isoforms are expressed specifically or predominantly in spermatogenic cells, often during the post-meiotic phase, and replace the ubiquitous isozymes that are also present in somatic cells
physiological function
-
PFKFB3 has a role in nuclear signaling
physiological function
-
spermatogenesis, both PFK-2 isozymes have specific roles in testis metabolism and physiology, PFK-2 isozyme expression switches from the ubiquitous form, required during proliferative phases, to the testicular form, which is the germ cell-specific one
physiological function
-
enzyme acts as an endogenous glucokinase activator. Binding and activation of glucokinase by bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in beta-cells is promoted by glucose, resulting in an enhancement of insulin secretion at stimulatory glucose concentrations, without affecting basal insulin secretion
physiological function
Q16877
enzyme is required to balance glycolytic activity and antioxidant production to maintain cellular redox balance in prostate cancer cells. Depletion of the enzyme inhibits tumor growth in a xenograft model, indicating that it is required under physiologic nutrient levels. Enzyme mRNA expression is greater in metastatic prostate cancer compared with primary tumors
physiological function
-
is an antagonist of glucokinase inhibition by the competitive glucokinase inhibitor mannoheptulose at increasing glucose concentrations. In combination with chemical activator LY2121260, the enzyme shows additive activation of glucokinase
physiological function
Q7TS91
knockdown of isoform PFKFB3/iPFK2 in N-43/5 neurons causes a decrease in rates of glycolysis, which is accompanied by increased AMP-activated protein kinase phosphorylation, increased agouti-related protein mRNA levels and decreased cocaine-amphetamine-related transcript mRNA levels. Overexpression of PFKFB3/iPFK2 in N-43/5 neurons causes an increase in glycolysis, which is accompanied by decreased AMP-activated protein kinase phosphorylation and decreased agouti-related protein mRNA levels and increased cocaine-amphetamine-related transcript mRNA levels
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + beta-D-fructose 2,6-bisphosphate
ATP + beta-D-fructose 6-phosphate
show the reaction diagram
-
reverse reaction, at 50% the rate of forward reaction
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P16118
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P16118
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q16875
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P25114
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q75IQ9
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
O81398
-
-
?, r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q9MB58
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
O64983
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q52MQ5, Q6PY95
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q16875
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q9JJH5
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P70265
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
via phosphorylenzyme intermediate
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
regulation of glycolysis
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
transfers gamma-phosphoryl group of ATP to hydroxyl group at C-2 of fructose 6-phosphate
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
transfers gamma-phosphoryl group of ATP to hydroxyl group at C-2 of fructose 6-phosphate, no substrates are diphosphate, glucose 6-phosphate
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
sugar phosphate specificity
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
not: ribose 5-phosphate
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
not: ribose 5-phosphate, not: 1-O-methyl-D-fructose 6-phosphate, alpha-/beta-methyl-D-fructofuranoside 6-phosphate, 2,5-anhydro-D-mannitol 6-phosphate, D-arabinose 5-phosphate
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q16875
the inducible enzyme is an important regulator of glycolysis that may be responsible for sustaining the high glycolytic flux of rapidly proliferating leukemia cells
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P25114
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P25114
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
O64983
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q52MQ5, Q6PY95
bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q16875
bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
carbon-partitioning in Arabidopsis is regulated by fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P16118
PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severe hypoxic conditions
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
site-directed mutant study and inhibition kinetics suggest that the reaction will be catalyzed most efficiently by the protein when the substrates bind to the active pocket in an ordered manner in which ATP binds first
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
activity determined spectrophotometrically by coupling the fructose-1,6-bisphosphate production to the oxidation of NADH
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli, role in the progression of cancerous cells, antiproliferative effects during inhibitor incubation determined
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q9JJH5
phosphorylation of PFK-2 on Ser-32, inhibition of hepatic glucose metabolism
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P70265
transgene causes changes in cardiac metabolite concentrations, increased glycolysis, reduced palmitate oxidation, protection from hypoxia
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-psicose 6-phosphate
?
show the reaction diagram
-
-
-
-
?
ATP + D-tagatose 6-phosphate
?
show the reaction diagram
-
-
-
-
?
ATP + L-sorbose 6-phosphate
?
show the reaction diagram
-
-
-
-
?
CTP + D-fructose 6-phosphate
CDP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
GTP + beta-D-fructose 6-phosphate
GDP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
GTP + beta-D-fructose 6-phosphate
GDP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
less effective than ATP
-
-
?
ITP + beta-D-fructose 6-phosphate
IDP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
MgATP2- + beta-D-fructose 6-phosphate
?
show the reaction diagram
-
-
-
-
-
MgATP2- + beta-D-fructose 6-phosphate
?
show the reaction diagram
-
-
-
-
-
MgATP2- + beta-D-fructose 6-phosphate
?
show the reaction diagram
-
-
-
-
-
MgATP2- + beta-D-fructose 6-phosphate
?
show the reaction diagram
-
-
-
-
-
MgATP2- + beta-D-fructose 6-phosphate
?
show the reaction diagram
-
-
-
-
-
MgATP2- + beta-D-fructose 6-phosphate
?
show the reaction diagram
-
-
-
-
-
UTP + D-fructose 6-phosphate
UDP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
MgATP2- + beta-D-fructose 6-phosphate
?
show the reaction diagram
-
analysis of MgATP-induced tetramer formation
-
-
?
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
P16118
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
P25114
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
O81398
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
Q9MB58
also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
-
-
-
additional information
?
-
-
isotope exchange reaction between ATP and ADP in the absence of fructose 6-phosphate
-
-
-
additional information
?
-
-
with discrete catalytic sites
-
-
-
additional information
?
-
-
with discrete catalytic sites
-
-
-
additional information
?
-
-
allosteric bifunctional enzyme, not heart
-
-
-
additional information
?
-
-
isotope exchange between fructose 6-phosphate and fructose 2,6-bisphosphate in the absence of adenine nucleotides
-
-
-
additional information
?
-
-
Cys-295 is involved in allosteric regulation
-
-
-
additional information
?
-
Q52MQ5, Q6PY95
evolution of the bifunctional enzyme
-
-
-
additional information
?
-
-
role of the enzyme in catalysis and regulation of glycolysis/gluconeogenesis and related enzymes, overview
-
-
-
additional information
?
-
Q16875
the bifunctional enzyme catalyzes the synthesis, 6-phosphofructo-2-kinase, and hydrolysis, fructose-2,6-bisphosphatase, of beta-D-fructose 2,6-bisphosphate, an activator of glycolysis and an inhibitor of gluconeogenesis
-
-
-
additional information
?
-
-
coordinate roles for glucokinase and PFK2 in the elevated hepatic glycolysis in fa/fa rats
-
-
-
additional information
?
-
-
it is unlikely that protein kinase Czeta is required for activation of 6-phosphofructo-2-kinase by insulin in heart
-
-
-
additional information
?
-
-
PFKFB3 is activated by mitogenic inflammatory and hypoxic stimuli. PFKFB4 controls glycolytic flux to lactate and the nonoxidatibe pentose shunt, and is selectively required for the tumorigenic growth of ras-transformed cells
-
-
-
additional information
?
-
-
sterol regulatory element binding protein-1a binds to a sterol regulatory element box and transcriptionally activates Sparus aurata liver PFKFB1
-
-
-
additional information
?
-
-
the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
-
-
-
additional information
?
-
O60825, Q16877
expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
-
-
-
additional information
?
-
-
mechanism of enzyme inhibition by ATP analyzed by structure determination
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P16118
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q75IQ9
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
O81398
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q9MB58
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q52MQ5, Q6PY95
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q16875
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q9JJH5
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P70265
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
-
regulation of glycolysis
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
Q16875
the inducible enzyme is an important regulator of glycolysis that may be responsible for sustaining the high glycolytic flux of rapidly proliferating leukemia cells
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P25114
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
enzyme plays an indirect yet key role in the regulation of glucose metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P25114
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
O64983
responsible for regulation of fructose 2,6-bisphosphate-concentration
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
enzyme plays an important role in the regulation of hepatic carbohydrate metabolism
-
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
carbon-partitioning in Arabidopsis is regulated by fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
P16118
PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severe hypoxic conditions
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
show the reaction diagram
-
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli
-
-
?
additional information
?
-
-
Cys-295 is involved in allosteric regulation
-
-
-
additional information
?
-
Q52MQ5, Q6PY95
evolution of the bifunctional enzyme
-
-
-
additional information
?
-
-
role of the enzyme in catalysis and regulation of glycolysis/gluconeogenesis and related enzymes, overview
-
-
-
additional information
?
-
Q16875
the bifunctional enzyme catalyzes the synthesis, 6-phosphofructo-2-kinase, and hydrolysis, fructose-2,6-bisphosphatase, of beta-D-fructose 2,6-bisphosphate, an activator of glycolysis and an inhibitor of gluconeogenesis
-
-
-
additional information
?
-
-
coordinate roles for glucokinase and PFK2 in the elevated hepatic glycolysis in fa/fa rats
-
-
-
additional information
?
-
-
it is unlikely that protein kinase Czeta is required for activation of 6-phosphofructo-2-kinase by insulin in heart
-
-
-
additional information
?
-
-
PFKFB3 is activated by mitogenic inflammatory and hypoxic stimuli. PFKFB4 controls glycolytic flux to lactate and the nonoxidatibe pentose shunt, and is selectively required for the tumorigenic growth of ras-transformed cells
-
-
-
additional information
?
-
-
sterol regulatory element binding protein-1a binds to a sterol regulatory element box and transcriptionally activates Sparus aurata liver PFKFB1
-
-
-
additional information
?
-
-
the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
Q16875
-
ATP
Q52MQ5, Q6PY95
; binding site of isozyme Tb1, overview
ATP
-
as MgATP2-
GMP
-
activation
IMP
-
activation
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
AsO43-
-
can replace phosphate; requirement
AsO43-
-
activation
Mg2+
-
MgATP2; MgGTP2
Mg2+
-
MgATP2
Mg2+
-
-
Mg2+
-
inhibition
Mg2+
-
MgATP2
Mg2+
-
inhibits at higher concentrations, strain DF903; MgATP2; MgGTP2; requirement, active substrate: MgNTP
Mg2+
-
K51 is essential for binding of Mg(mantATP)
Mg2+
-
inhibition of enzyme at 2 mM, but no effect on activation by ATP
Mg2+
Q16875
-
Mg2+
Q52MQ5, Q6PY95
;
Mg2+
-
as MgATP2-
Mg2+
-
requirement of a Mg2+ ion, besides the one present in the metal-nucleotide complex, for catalysis in the wild-type enzyme
Mg2+
-
required for activity
Mg2+
-
required for activity, MgATP is the active substrate
phosphate
-
requirement
phosphate
-
-
phosphate
-
-
phosphate
-
liver enzyme
phosphate
-
requirement
phosphate
-
requirement
phosphate
Q9MB58
-
phosphate
-
activation
phosphate
-
requirement
phosphate
-
-
phosphate
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,5-anhydro-D-mannitol 6-phosphate
-
-
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
(3PO), small-molecule inhibitor, mixed inhibition mechanism, both competitive and uncompetitive inhibition, suppresses glycolytic flux and is cytostatic to neoplastic cells, inhibits activity of recombinantly expressed PFKFB3
3-phosphoglycerate
O64983
-
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
Q9JJH5
AICAR, associated with phosphorylation of PFK-2 on Ser-32, phosphorylation increased of both wild-type and overexpressed PFK-2 protein in hepatocytes
ADP
-
product inhibition
AMP
Q9MB58
not
ATP
-
at low concentrations of Mg2+ and fructose 6-phosphate
ATP
-
free form
ATP
Q9MB58
not
beta-D-fructose 2,6-bisphosphate
-
product inhibition
beta-D-fructose 2,6-bisphosphate
-
kinetics
beta-D-fructose 2,6-bisphosphate
-
-
beta-D-fructose 6-phosphate
Q16875
modeling of beta-D-fructose 6-phosphate as inhibitor
citrate
-
not
citrate
-
heart enzyme is more sensitive than liver enzyme
citrate
-
at physiological concentrations
citrate
-
skeletal muscle enzyme is more sensitive than liver enzyme
citrate
-
phosphorylation enhances sensitivity
citrate
-
weak
citrate
-
-
citrate
Q52MQ5, Q6PY95
60% inhibition at 1 mM
citrate
-
strong
dihydroxyacetone phosphate
-
weak
dihydroxyacetone phosphate
Q9MB58
-
dihydroxyacetone phosphate
O64983
-
diphosphate
-
-
diphosphate
-
-
diphosphate
-
not phosphate
diphosphate
-
not phosphate
diphosphate
Q9MB58
not phosphate
diphosphate
O64983
not phosphate
Glucagon
-
the native and the recombinant wild-type and mutant enzymes are phosphorylated after incubation with glucagon inactivating the enzyme
Glucagon
Q9JJH5
phosphorylation of PFK2 on Ser-32 in liver
glycerate 2-phosphate
Q9MB58
-
glycerate 2-phosphate
-
-
Glycerol 2-phosphate
-
-
glycerol 3-phosphate
Q52MQ5, Q6PY95
20% inhibition at 2mM
glycolate 2-phosphate
-
-
guanidine
-
inactivation, unfolding
m-periodate
-
strong, DTT protects or reverses
Mg2+
-
MgATP
MgATP
-
inhibited by, structure determination reveals substrate inhibition due to sequential binding of two MgATP molecules per subunit, the first at the usual site occupied by the nucleotide in homologous enzymes and the second at the allosteric site, making a number of direct and Mg-mediated interactions with the first, two configurations observed for the second MgATP, one of which involves interactions with Tyr-23 from the adjacent subunit in the dimer and the other making an unusual non-Watson-Crick base pairing with the adenine in the substrate ATP
MgATP2-
-
allosteric inhibition, important regulation of in vivo carbohydrate metabolism under gluconeogenic conditions
MgATP2-
-
E190Q mutant presents alterations in the inhibition by MgATP2- and phosphate
MgATP2-
-
allosteric inhibition
MgNTP
-
strain DF903, substrate inhibition, most effective: MgATP2, at low fructose concentration
-
N-(1-pyrenil)maleimide
-
complete loss of catalytic activity, but modified enzyme is able to bind beta-D-fructose 6-phosphate, the presence of MgATP2- completely protects the enzyme activity, the modified enzyme elutes as a monomer
N-Bromoacetylethanolamine
-
repetitive administration affects inhibition of glycolysis and lipid metabolism, causing suppression of body weight gain
N-Bromoacetylethanolamine
-
specific active site-directed inactivator of enzyme, in vitro and in vivo
o-phthalaldehyde
-
kinetics, DTT or substrates do not protect
phosphate
-
inhibits wild-type and mutant enzym E190Q. E190 contributs to the mechanism of phosphate inhibition in Pfk-2. E190Q mutant presents alterations in the inhibition by MgATP2- and phosphate
phosphoenolpyruvate
-
kinetics
phosphoenolpyruvate
-
not
phosphoenolpyruvate
-
mixed-type inhibitory effect, phosphorylation enhances sensitivity
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
weak
phosphoenolpyruvate
Q9MB58
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
Q16875
HBP1 and HBP2, the bifunctional enzyme is regulated via inhibition by phosphoenolpyruvate, uncompetitive against ATP, noncompetitive against beta-D-fructose 6-phosphate
phosphoenolpyruvate
Q52MQ5, Q6PY95
-
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
strong
protein kinase A
Q52MQ5, Q6PY95
inactivation via a 7fold increase in Km for fructose 6-phosphate without alteration of Vmax
-
pyrene maleimide
-
incorporation of 2 mol per mol of enzyme subunit, modifiying Cys-238 and Cys-295, leads to rapid inactivation, MgATP2- protects Cys295, modification of Cys238 does not abolish activity
sn-glycerol 3-phosphate
-
stimulates phosphatase activity
sn-glycerol 3-phosphate
-
heart enzyme is less sensitive than liver
sn-glycerol 3-phosphate
-
i.e. alpha-glycerol phosphate
sn-glycerol 3-phosphate
-
-
sn-glycerol 3-phosphate
-
not
sn-glycerol 3-phosphate
-
heart enzyme is less sensitive than liver
sn-glycerol 3-phosphate
-
heart enzyme is less sensitive than liver; liver enzyme
sn-glycerol 3-phosphate
-
most potent inhibitor of phosphorylated liver enzyme, phosphorylation enhances sensitivity
sn-glycerol 3-phosphate
Q9MB58
-
sn-glycerol 3-phosphate
-
most potent inhibitor of phosphorylated liver enzyme, phosphorylation enhances sensitivity; skeletal muscle enzyme is not sensitive to inhibition
sn-glycerol 3-phosphate
-
-
sn-glycerol 3-phosphate
-
75% decrease in activity of liver enzyme but not hepatoma cells
sn-glycerol 3-phosphate
-
not
additional information
-
phosphorylation at lower pH-values; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation site: Ser-32
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation of foetal liver enzyme by protein kinase C, but no effect on adult liver cells
-
additional information
-
not: cAMP or protein kinase alone; phosphorylation at pH 6.6, not at pH 8; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation by cAMP-dependent protein kinase of liver enzyme, not of skeletal muscle enzyme, since the phosphorylation site target Ser-32 of the liver isozyme is replaced by Ala in the muscle isozyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase, but not rat skeletal muscle, bovine and rat heart enzyme
-
additional information
-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
-
additional information
-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
-
additional information
-
no inhibition by lactate, glyceraldehyde 3-phosphate, beta-D-fructose 1,6-bisphosphate
-
additional information
-
phosphorylation by cAMP-dependent protein kinase, but no inhibition
-
additional information
-
-
-
additional information
-
no inhibition by protein kinase C; phosphorylation by cAMP-dependent protein kinase, but no inhibition
-
additional information
-
not: ITP, GTP, UTP, CTP, strain DF905; phosphorylation by cAMP-dependent protein kinase causes inactivation
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not of heart and skeletal muscle enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation
-
additional information
-
loss of phosphorylation-dependent reduction of enzyme by deletion of the N-terminal residues of enzyme. The deletion of 7 N-terminal amino acids causes a 75% decrease in activity; phosphorylation site: Ser-32
-
additional information
-
phosphorylation site: Ser-32
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not skeletal muscle enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes 35% inactivation of isozyme L of adipose tissue, not isozyme M
-
additional information
-
kinetic of phosphorylation by cAMP-dependent protein kinase
-
additional information
Q52MQ5, Q6PY95
enzyme is not affected by protein kinase C
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes 80% decrease in activity of the liver cells but not of hepatoma cells; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not of kidney, testis and heart enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
-
additional information
-
-
-
additional information
-
the islet enzyme lacks protein kinase A and C phosphorylation sites
-
additional information
-
no inhibition by phosphorylation with Ca2+/calmodulin dependent protein kinase; no inhibition by protein kinase C
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
the binding of ATP to the fructose 2,6-bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase leads to activation of enzyme, but no activation of rat liver enzyme
glucose
-
inhibition by N-bromoacetylethanolamine
Insulin
-
activation of transfected heart enzyme in human embryonic kidney 293 cells by inducing the phosphorylation of Ser466 and Ser483, activation is mediated by 3-phosphoinositide-dependent kinase-1, protein kinase B is in vivo not essential, activation is sensitive to LY294002 and wortmannin and insensitive to rapaycin and PD98059
-
iodoacetamide
-
-
pyruvate
Q9MB58
-
iodoacetamide
-
activation, kidney and liver, not heart or testis enzyme
additional information
-
one enzyme form is activated dramatically as result of modification by MgATP during preincubation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00087
ATP
-
mutant enzyme A44G
0.0169
ATP
-
wild-type enzyme
0.018
ATP
-
pH 7.5, 30C, in presence of phosphate
0.048
ATP
-
pH 7.5, 30C, comparison of Km of skeletal muscle and liver enzyme
0.048
ATP
-
pH 7.5, 25C, heart
0.055
ATP
-
pH 7.1, 30C
0.06
ATP
-
strain DF903
0.061
ATP
-
pH 7.5, 30C, liver
0.083
ATP
-
pH 7.5, 25C, heart
0.1
ATP
-
pH 7.5, 30C
0.1
ATP
-
pH 7.5, 30C, MgATP
0.1
ATP
-
pH 7.5, 30C, in absence of phosphate
0.1
ATP
-
pH 7.5, 30C, testis
0.1
ATP
-
-
0.1
ATP
-
pH 7.5, 25C, testis
0.11
ATP
-
pH 7.5, 30C
0.12 - 0.36
ATP
-
pH 7.8
0.12 - 0.36
ATP
-
pH 7.5, 30C, kinetic study
0.12 - 0.36
ATP
-
pH 7.5, 30C, kinetic study
0.12 - 0.36
ATP
-
pH 8.2, 30C, strain DF905
0.14
ATP
-
mutant enzyme A44V
0.19
ATP
-
pH 8.5, 30C, foetal enzyme
0.19
ATP
Q9MB58
pH 6.0, 25C
0.195
ATP
-
pH 8.5, 30C, adult enzyme
0.2
ATP
-
pH 7.5, 22C
0.22
ATP
-
pH 7.5, 30C
0.223
ATP
-
pH 7.4, 30C, presence of phosphate
0.226
ATP
-
pH 7.5, 30C, absence of phosphate
0.26
ATP
-
-
0.26
ATP
-
pH 7.5, 30C
0.29 - 0.38
ATP
-
pH 7.1, 30C, kinetic data of various enzyme forms
0.31
ATP
-
pH 7.5, 25C, liver
0.328
ATP
-
pH 7.5, 25C, islet
0.4
ATP
-
pH 6.6, 25C
0.4
ATP
-
pH 7.8
0.5
ATP
-
pH 8.0, three forms
0.62 - 0.7
ATP
-
-
0.7
ATP
-
pH 7.5, 30C, isozyme I
0.88
ATP
Q52MQ5, Q6PY95
30C
1.32
ATP
O64983
pH 7.8, 25C, effect of phosphate on Km
1.62
ATP
Q52MQ5, Q6PY95
pH 7.1, 30C, recombinant isozyme Tb1
0.02
beta-D-fructose 2,6-bisphosphate
-
pH 7.5, 30C
0.21
beta-D-fructose 2,6-bisphosphate
-
pH 7.4, 30C, in presence of phosphate
0.0038
beta-D-fructose 6-phosphate
-
mutant enzyme A44G
0.006
beta-D-fructose 6-phosphate
-
pH 7.5, 30C and heating at 90C for 10 min, with ATP, in presence of phosphate
0.0064
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant non-phosphorylated, HBP1 mutant S477D
0.0066
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant non-phosphorylated, HBP1 mutants T470D and S460D/T470D
0.0067
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant non-phosphorylated, HBP1 mutant S460D
0.0071
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant non-phosphorylated, HBP1 mutant H253A/S460D; pH 7.5, 30C, recombinant non-phosphorylated, wild-type HBP1
0.0073
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant non-phosphorylated, HBP1 mutant H253A
0.0074
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant non-phosphorylated, His-tagged wild-type HBP2
0.008
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant non-phosphorylated, His-tagged wild-type HBP1
0.0092
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant Hnon-phosphorylated, is-tagged HBP1 deletion mutant
0.0095
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant non-phosphorylated, His-tagged HBP1 mutant S302R
0.0102
beta-D-fructose 6-phosphate
-
wild-type enzyme
0.013
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant His-tagged chimeric mutant enzyme, phosphorylated or nonphosphorylated
0.016
beta-D-fructose 6-phosphate
-
pH 7.5, 30C, kinetic study
0.016
beta-D-fructose 6-phosphate
-
pH 7.5, 25C, liver
0.017
beta-D-fructose 6-phosphate
-
pH 7.5, 25C, islet
0.019 - 0.021
beta-D-fructose 6-phosphate
-
pH 7.8, in presence of phosphate
0.02 - 0.03
beta-D-fructose 6-phosphate
-
pH 7.5, 30C, in presence of phosphate
0.02
beta-D-fructose 6-phosphate
-
C-terminal deletion mutant D299, 1 mM co-substrate
0.022
beta-D-fructose 6-phosphate
-
pH 7.5, 30C, comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.023
beta-D-fructose 6-phosphate
-
comparison of Km of wild-type, mutant and mutant phosphorylated enzyme; pH 7.5, 25C, heart
0.023
beta-D-fructose 6-phosphate
-
comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.023
beta-D-fructose 6-phosphate
-
pH 7.5, 25C, heart
0.025
beta-D-fructose 6-phosphate
-
pH 7.5, 30C, liver, comparison of Km of wild-type, mutant and mutant phosphorylated enzyme
0.027
beta-D-fructose 6-phosphate
-
pH 7.1, 30C
0.029
beta-D-fructose 6-phosphate
-
L307A, C-terminal point mutant, 1 mM co-substrate
0.031
beta-D-fructose 6-phosphate
-
recombinant wild-type enzyme and mutant C238A
0.032
beta-D-fructose 6-phosphate
-
pH 7.5, 30C
0.035
beta-D-fructose 6-phosphate
-
pH 7.5, 30C
0.036
beta-D-fructose 6-phosphate
-
C-terminal deletion mutant A305, 1 mM co-substrate
0.04
beta-D-fructose 6-phosphate
-
pH 7.5, 30C, wild-type enzyme, testis
0.04
beta-D-fructose 6-phosphate
-
pH 7.5, 25C, testis
0.044
beta-D-fructose 6-phosphate
-
pH 8.5, 30C, foetal liver enzyme
0.047
beta-D-fructose 6-phosphate
-
pH 8.5, 30C, adult liver enzyme
0.047
beta-D-fructose 6-phosphate
-
recombinant mutant C238F
0.05
beta-D-fructose 6-phosphate
-
pH 7.5, 30C, with ATP, in presence of phosphate
0.05
beta-D-fructose 6-phosphate
-
pH 7.5, 30C
0.05
beta-D-fructose 6-phosphate
-
-
0.05
beta-D-fructose 6-phosphate
-
pH 7.1, 30C, MgATP2-, phosphorylated chicken enzyme
0.056
beta-D-fructose 6-phosphate
-
pH 7.5, 30C, comparison of Km of skeletal muscle and liver enzyme
0.056
beta-D-fructose 6-phosphate
-
pH 7.5, 25C, muscle
0.057
beta-D-fructose 6-phosphate
-
wild-type, 1 mM co-substrate, chosen in order avoid the effect of MgATP binding at the allosteric site to the binding of fructose-6-P to the catalytic site, that is observed above 1 mM MgATP
0.058
beta-D-fructose 6-phosphate
-
native enzyme
0.06
beta-D-fructose 6-phosphate
-
C-terminal deletion mutant L307, 1 mM co-substrate
0.062
beta-D-fructose 6-phosphate
-
Y306A, C-terminal point mutant, 1 mM co-substrate
0.063
beta-D-fructose 6-phosphate
-
C238-pyrene maleimide modified enzyme
0.07
beta-D-fructose 6-phosphate
-
pH 7.5, 30C
0.081
beta-D-fructose 6-phosphate
-
recombinant mutant C295F
0.088
beta-D-fructose 6-phosphate
-
recombinant mutant C295A
0.09
beta-D-fructose 6-phosphate
-
pH 6.6, 25C
0.097
beta-D-fructose 6-phosphate
-
-
0.1
beta-D-fructose 6-phosphate
-
pH 7.5, 30C
0.1
beta-D-fructose 6-phosphate
-
pH 7.5, 30C
0.12
beta-D-fructose 6-phosphate
-
pH 7.8
0.14
beta-D-fructose 6-phosphate
-
pH 7.5, 30C
0.156
beta-D-fructose 6-phosphate
-
pH 7.5, 30C, with ATP, in presence of phosphate
0.204
beta-D-fructose 6-phosphate
-
mutant enzyme A44V
0.33 - 0.4
beta-D-fructose 6-phosphate
-
pH 7.1, 30C, kinetic data of various enzyme forms
0.37
beta-D-fructose 6-phosphate
-
-
0.4
beta-D-fructose 6-phosphate
-
pH 7.1, 37C
0.5 - 1
beta-D-fructose 6-phosphate
-
pH 8.0, forms 1-3, kinetic data of various enzyme forms
0.5
beta-D-fructose 6-phosphate
-
pH 7.5, 22C
0.5
beta-D-fructose 6-phosphate
Q9MB58
pH 6.0, 25C
0.6
beta-D-fructose 6-phosphate
-
-
0.94
beta-D-fructose 6-phosphate
-
pH 7.4, 30C, presence of phosphate
1 - 1.1
beta-D-fructose 6-phosphate
-
pH 7.8, absence of phosphate
1 - 1.1
beta-D-fructose 6-phosphate
-
pH 7.5, 30C, in absence of phosphate
1 - 1.1
beta-D-fructose 6-phosphate
-
pH 8.2, 30C, ITP, strain DF905
1.4
beta-D-fructose 6-phosphate
-
pH 7.5, 30C, with ATP, absence of phosphate
1.4
beta-D-fructose 6-phosphate
O64983
pH 7.8, 25C, effect of phosphate on Km
1.9 - 4.6
beta-D-fructose 6-phosphate
Q52MQ5, Q6PY95
pH 7.1, 30C, recombinant isozyme Tb1
5.8
beta-D-fructose 6-phosphate
Q52MQ5, Q6PY95
pH 7.1, 30C
39
beta-D-fructose 6-phosphate
Q52MQ5, Q6PY95
pH 7.1, 30C, protein kinase A treated enzyme
0.9
CTP
-
pH 8.2, 30C, strain DF903
2
CTP
-
pH 8.2, 30C, strain DF905
0.0094
D-fructose 6-phosphate
-
mutant enzyme E190Q, 30 mM Mg2+
0.01
D-fructose 6-phosphate
-
mutant enzyme E190Q, 1 mM Mg2+
0.028
D-fructose 6-phosphate
-
wild-type enzyme, 30 mM Mg2+
0.1
D-fructose 6-phosphate
-
wild-type enzyme, 1 mM Mg2+
7.4
D-psicose 6-phosphate
-
pH 7.5, 30C
15
D-tagatose 6-phosphate
-
pH 7.5, 30C
0.35
GTP
-
pH 8.2, 30C, strain DF903
1.5
GTP
-
pH 8.2, 30C, strain DF905
0.3
ITP
-
pH 8.2, 30C, strain DF903
0.175
L-Sorbose 6-phosphate
-
pH 7.5, 30C
0.0072
MgATP2-
-
pH 7.1, 30C, phosphorylated enzyme
0.0095 - 0.012
MgATP2-
-
pH 7.5, 30C
0.0095 - 0.012
MgATP2-
-
pH 7.1, 30C, native pigeon enzyme
0.01
MgATP2-
-
C-terminal deletion mutant L307, 1 mM co-substrate
0.0107
MgATP2-
-
recombinant mutant C295F
0.0137
MgATP2-
-
Y306A, C-terminal point mutant, 1 mM co-substrate
0.015
MgATP2-
-
wild-type, 1 mM co-substrate
0.017
MgATP2-
-
recombinant wild-type enzyme and mutant C238A
0.02
MgATP2-
-
wild-type enzyme, 1 mM Mg2+
0.021
MgATP2-
-
recombinant mutant C238F
0.022
MgATP2-
-
wild-type enzyme, 30 mM Mg2+
0.042
MgATP2-
-
native enzyme
0.044
MgATP2-
-
C238-pyrene maleimide modified enzyme
0.061
MgATP2-
-
recombinant mutant C295A
0.149
MgATP2-
-
mutant enzyme E190Q, 1 mM Mg2+
0.29
MgATP2-
-
pH 7.1, 30C, native chicken enzyme
0.32
MgATP2-
-
mutant enzyme E190Q, 30 mM Mg2+
0.5
MgATP2-
-
-
0.5
MgATP2-
-
pH 7.5, 30C
0.5
MgATP2-
-
pH 7.5, 30C
0.8
MgATP2-
-
C-terminal deletion mutant A305, 1 mM co-substrate
0.88
MgATP2-
-
C-terminal deletion mutant Y306, 1 mM co-substrate
0.954
MgATP2-
-
L307A, C-terminal point mutant, 1 mM co-substrate
0.78
UTP
-
pH 8.2, 30C, strain DF903
2.3
UTP
-
pH 8.2, 30C, strain DF905
2
MgATP2-
-
C-terminal deletion mutant D299, 1 mM co-substrate
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
-
-
-
additional information
additional information
Q9MB58
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
-
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
-
-
-
additional information
additional information
-
comparison of Km of wild-type and mutant enzyme
-
additional information
additional information
Q16875
recombinant wild-type and mutant enzymes, Km for phosphorylated wild-type enzyme and mutants with beta-D-fructose 6-phosphate and beta-D-fructose 2,6-bisphosphate, kinetics, modeling
-
additional information
additional information
-
kinetics of native and pyrene maleimide modified enzyme
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes
-
additional information
additional information
-
kinetic data of native and phosphorylated enzyme
-
additional information
additional information
-
comparison of Km of hepatoma cells and liver enzyme
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
ATP
-
wild-type enzyme
0.17
ATP
-
mutant enzyme A44V
0.19
ATP
-
mutant enzyme A44G
0.14
beta-D-fructose 6-phosphate
-
wild-type enzyme
0.17
beta-D-fructose 6-phosphate
-
mutant enzyme A44V
0.19
beta-D-fructose 6-phosphate
-
mutant enzyme A44G
0.391
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant HBP1 mutant H253A
0.394
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant HBP1 mutant S460D; pH 7.5, 30C, recombinant HBP1 mutant S460D/T470D
0.399
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant His-tagged HBP1 mutant S302R
0.401
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant HBP1 mutant H253A/S460D
0.405
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant HBP1 mutant S477D
0.407
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant wild-type HBP1
0.43
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant His-tagged wild-type HBP1
0.435
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant HBP1 mutant T470
0.447
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant His-tagged wild-type HBP2
0.654
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant non-phosphorylated, His-tagged chimeric mutant enzyme
0.678
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant phosphorylated, His-tagged chimeric mutant enzyme
0.696
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant His-tagged HBP1 deletion mutant
13
beta-D-fructose 6-phosphate
-
recombinant mutant C295A
39
beta-D-fructose 6-phosphate
-
recombinant mutant C295F
70
beta-D-fructose 6-phosphate
-
recombinant mutants C238A and C238F
90
beta-D-fructose 6-phosphate
-
recombinant wild-type enzyme
9240
beta-D-fructose 6-phosphate
-
native enzyme
9320
beta-D-fructose 6-phosphate
-
C238-pyrene maleimide modified enzyme
0.14
D-fructose 6-phosphate
-
mutant enzyme E190Q, 1 mM Mg2+
1.43
D-fructose 6-phosphate
-
mutant enzyme E190Q, 30 mM Mg2+
53
D-fructose 6-phosphate
-
wild-type enzyme, 1 mM Mg2+; wild-type enzyme, 30 mM Mg2+
0.14
MgATP2-
-
mutant enzyme E190Q, 1 mM Mg2+
1.43
MgATP2-
-
mutant enzyme E190Q, 30 mM Mg2+
13
MgATP2-
-
recombinant mutant C295F
39
MgATP2-
-
recombinant mutant C295A
53
MgATP2-
-
wild-type enzyme, 1 mM Mg2+; wild-type enzyme, 30 mM Mg2+
70
MgATP2-
-
recombinant mutants C238A and C238F
90
MgATP2-
-
recombinant wild-type enzyme
9240
MgATP2-
-
native enzyme
9320
MgATP2-
-
C238-pyrene maleimide modified enzyme
additional information
additional information
-
comparison of kcat/Km values of wild-type and mutant enzymes
-
additional information
additional information
-
comparison of kcat/Km values of wild-type and mutant enzymes
-
additional information
additional information
Q16875
kcat of wild-type and mutant HBP1 and of HBP2 with beta-D-fructose 2,6-bisphosphate, kcat for phosphorylated wild-type enzyme and mutants with beta-D-fructose 6-phosphate and beta-D-fructose 2,6-bisphosphate
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.095
2,5-anhydro-D-mannitol 6-phosphate
-
pH 7.5, 30C
0.025
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
inhibition of recombinant PFKFB3 protein, no inhibition of purified PFK-1 activity
0.16
ADP
-
pH 6.6, 25C
0.008
ATP
-
pH 8.2, 30C, mutant strain DF905
0.01
ATP
-
pH 8.2, 30C, mutant strain DF903
8.5
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant HBP1 mutant S460D/T470D
9.2
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant HBP1 mutant S460D
9.5
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant HBP1 mutant H253A/S460D
9.6
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant His-tagged HBP1 deletion mutant
9.7
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant HBP1 mutant S477D
9.9
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant wild-type HBP1
10.9
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant His-tagged HBP1 mutant S302R
11.1
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant HBP1 mutant H253A
11.8
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant His-tagged wild-type HBP2
12.2
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant His-tagged wild-type HBP1
12.7
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant non-phosphorylated, His-tagged chimeric mutant enzyme
13
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant HBP1 mutant T470
13.4
beta-D-fructose 6-phosphate
Q16875
pH 7.5, 30C, recombinant phosphorylated, His-tagged chimeric mutant enzyme
0.025
citrate
-
hepatoma cells
0.026
citrate
-
liver
0.035
citrate
-
-
0.083
citrate
-
pH 7.1, 30C, native enzyme
0.084
citrate
-
pH 7.1, 30C, phosphorylated enzyme
0.12
citrate
-
pH 7.4, 30C
0.13
citrate
-
pH 7.1, 30C, phosphorylated enzyme
0.14
citrate
-
skeletal muscle
0.15
citrate
-
heart
0.2
citrate
-
liver
0.49
citrate
-
pH 7.1, 30C, native enzyme
0.55
citrate
-
pH 7.5, 30C
0.25
dihydroxyacetone phosphate
-
L form, pH 7.8, 30C
0.737
dihydroxyacetone phosphate
O64983
pH 7.8, 25C
1.35
dihydroxyacetone phosphate
Q9MB58
pH 6.0, 25C
1.9
dihydroxyacetone phosphate
-
H form, pH 7.8, 30C
0.026
diphosphate
-
L form, pH 7.8, 30C
0.106
diphosphate
O64983
pH 7.8, 25C
0.16
diphosphate
-
H form, pH 7.8, 30C
0.016
glycerate 2-phosphate
-
L form, pH 7.8, 30C
0.029
glycerate 2-phosphate
O64983
pH 7.8, 25C
0.14
glycerate 2-phosphate
-
H form, pH 7.8, 30C
0.45
glycerate 2-phosphate
Q9MB58
pH 6.0, 25C
0.084
Glycerate 3-phosphate
O64983
pH 7.8, 25C
0.02
glycolate 2-phosphate
-
L form, pH 7.8, 30C
2
N-Bromoacetylethanolamine
-
pH 7.5, 30C, recombinant testis enzyme
15
N-Bromoacetylethanolamine
-
pH 7.5, 30C, crude liver extracts
0.028
o-phthalaldehyde
-
pH 7.4, room temperature
0.014
phosphoenolpyruvate
-
pH 7.5, 30C, testis
0.018
phosphoenolpyruvate
-
L form, pH 7.8, 30C
0.045
phosphoenolpyruvate
O64983
pH 7.8, 25C
0.08
phosphoenolpyruvate
-
pH 7.5, 30C, liver
0.08
phosphoenolpyruvate
-
pH 7.5, 25C, islet
0.1
phosphoenolpyruvate
-
pH 7.5, 30C, heart
0.12
phosphoenolpyruvate
-
hepatoma cells
0.13
phosphoenolpyruvate
Q9MB58
pH 6.0, 25C
0.15
phosphoenolpyruvate
-
H form, pH 7.8, 30C
0.17
phosphoenolpyruvate
-
noncompetitive to ATP, pH 7.5, 30C
0.2
phosphoenolpyruvate
-
liver
0.23
phosphoenolpyruvate
-
pH 7.4, 30C
0.53
phosphoenolpyruvate
-
noncompetitive to fructose 6-phosphate, pH 7.5, 30C
0.7
phosphoenolpyruvate
Q52MQ5, Q6PY95
30C
2
phosphoenolpyruvate
-
30C
2.3
phosphoenolpyruvate
-
pH 6.6, 25C
0.018
sn-glycerol 3-phosphate
-
L form, pH 7.8, 30C
0.15
sn-glycerol 3-phosphate
-
pH 7.1
0.16
sn-glycerol 3-phosphate
-
H form, pH 7.8, 30C
0.35
sn-glycerol 3-phosphate
Q9MB58
pH 6.0, 25C
8.07
sn-glycerol 3-phosphate
O64983
pH 7.8, 25C
0.18
glycolate 2-phosphate
-
H form, pH 7.8, 30C
additional information
additional information
-
kinetic study
-
additional information
additional information
-
-
-
additional information
additional information
-
comparison of Ki for MgATP2- inhibition at different free Mg2+ concentrations
-
additional information
additional information
-
guanidine-inhibition of wild-type and mutant enzymes
-
additional information
additional information
-
comparison of Ki of wild type and mutant enzymes
-
additional information
additional information
Q16875
modeling of inhibition of HBP1 and HBP2 by phosphoenolpyruvate and beta-D-fructose 6-phosphate, Km for phosphorylated wild-type enzyme and mutants with beta-D-fructose 6-phosphate and beta-D-fructose 2,6-bisphosphate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00031
-
skeletal muscle
0.00295
-
heart
0.0104 - 0.0159
O64983
-
0.011
Q52MQ5, Q6PY95
purified enzyme
0.021
-
liver
0.04
-
-
0.042
-
-
0.055
-
adult
0.068
-
-
0.075
-
-
0.08
-
foetal
0.092
-
-
0.11
-
-
0.142
-
-
0.2
Q16875
recombinant purified HBP1 from Escherichia coli
0.277
-
specific PFK-2 activity of the recombinant PFKFB3 protein determined by measurement of fructose 2,6-bisphosphate
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
Q52MQ5, Q6PY95
-
additional information
O60825, Q16877
expression analysis in different tumor specimens with high and low malignity grade, RT-PCR and Western blot; expression analysis in different tumor specimens with high and low malignity grade, RT-PCR and Western blot; expression analysis in different tumor specimens with high and low malignity grade, RT-PCR and Western blot; proto-oncogenic character of the PFK-2/FBPase-2 of the PFKFB3 gene assumed to play a critical role in tumorigenesis, expression analyzed by RT-PCR and Western blot, expression up-regulated in astrocytomas with high malignity grade
additional information
Q75IQ9
located on chromosome 3, RNAi mutant analyzed, at the end of day, sucrose contents increased in leaves, fructose 6-phosphate 2-kinase activities and fructose 2,6-bisphosphate levels declined, involvement in the regulation of sucrose synthesis by controlling the levels of fructose 2,6-bisphosphate during the daytime; OsF2KP1 protein located on chromosome 5, transposon insertion mutant analyzed, expression of the corresponding gene inhibited mainly in leaves, at the end of day, sucrose contents increased in leaves, fructose 6-phosphate 2-kinase activities and fructose 2,6-bisphosphate levels declined, involvement in the regulation of sucrose synthesis by controlling the levels of fructose 2,6-bisphosphate during the daytime
additional information
Q9JJH5
inhibition of glucose-induced translocation, 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR) associated with phosphorylation of PFK2 on Ser-32, increase of phosphorylation less than that caused by glucagon, expression of PFK-2 mutant that lacks Ser-32 (PFK2-M) reverses inhibitory effects on glucokinase translocation
additional information
P70265
generation of transgenic mice with chronically elevated glycolysis by cardiac-specific overexpression of PFK-2, measurements of metabolites reveal 3fold elevated levels of fructose 2,6-bisphosphate, expression studies by real-time PCR and Western blot analysis, transgene causes significant increase in glycolysis providing acute benefits against hypoxia
additional information
Q16875
diet-induced obesity in transgenic mice, liver and plasma metabolites in transgenic and control mice, human Pfkfb3-specific gene probe used to quantify transgene overexpression by RT-PCR, measurement of fructose 2,6-bisphosphate levels in the liver, immunostaining and gene expression analysis in livers of transgenic and control mice, changes in hepatic gene expression profiles for key gluconeogenic and lipogenic enzymes, accumulation of lipids in periportal cells, gain in weight
additional information
-
binding of MgATP to an allosteric site provokes inhibition and a dimer-tetramer conversion of the enzyme, mutant generation by successive deletions of up to 10 residues and point mutations at the C-terminal end, elevated KM values for MgATP that fails to show the dimer-tetramer conversion, Y306 required for the quaternary packing involved in the dimer-tetramer conversion, the following residue L307 is crucial for the ternary packing necessary for the catalytic MgATP-binding site, dimer-tetramer conversion can be uncoupled from the conformational changes that lead to the MgATP-induced allosteric inhibition
additional information
-
monomer structure and structural features of intersubunit interactions, interactions with ligands at the active site, structure determination in its inhibited tetrameric form, with each subunit bound to two ATP molecules and two Mg ions, allosteric site reported for ATP, analogous structural features in the 6-phosphofructokinases from Escherichia coli compared
additional information
A7UAK4, A7UAK5, A7UAK6
identification and expression of alternative splice variants in different tissue under hypoxia, splice variants different at C-terminal region but catalytical domains of 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase identical, tissue-specific expression, different induction under hypoxic conditions, role of splice isoforms in cell adaptation to hypoxic conditions discussed; identification and expression of alternative splice variants in different tissue under hypoxia, splice variants different at C-terminal region but catalytical domains of 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase identical, tissue-specific expression, different induction under hypoxic conditions, role of splice isoforms in cell adaptation to hypoxic conditions discussed; identification and expression of alternative splice variants in different tissue under hypoxia, splice variants different at C-terminal region but catalytical domains of 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase identical, tissue-specific expression, different induction under hypoxic conditions, role of splice isoforms in cell adaptation to hypoxic conditions discussed
additional information
-
activity recovery after refolding is 90% in the full range of GdnHCl concentrations of 0.1-5.5 M guanidine hydrochloride
additional information
-
nuclei isolated from cells transfected with wild type PFKFB3 exhibit 6-phosphofructo-2-kinase activity that is significantly higher than the nuclei obtained from both vector and K472A/K473A-transfected cells
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
of 54000 Da and 58000 Da isozymes
6
Q52MQ5, Q6PY95
about
6.6
-
in the presence of phosphate
6.6
-
-
7 - 7.5
Q16875
assay at
7.1
Q52MQ5, Q6PY95
assay at
7.3 - 8.4
-
wild-type enzyme
7.4 - 7.9
-
-
7.5 - 8
-
native enzyme
7.5
-
native enzyme, absence of phosphate
7.5
-
25 mM phosphate
7.5
-
assay at
8
-
after incubation with cAMP-dependent protein kinase
8.4
-
5 mM phosphate
8.5
-
skeletal muscle
8.5
-
bovine
9.3
-
muscle-type isozyme
additional information
-
biphasic pH profile with two optima at pH 6.8 and 10.00 and a minimum at 8.5, comparison of pH optima of N- and C-deletion mutants of enzyme, comparison of kinetic properties of wild-type and deletion mutants at pH 6.8 and pH 8.2
additional information
-
comparison of pH-profiles of wild-type and mutant enzymes
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
-
continuous increase of activity from pH 5.5 with 70% of maximal activity to maximal activity from pH 7.5 to 8.5, phosphorylated enzyme
6 - 10
-
-
6 - 10
-
about 80% of maximal activity at pH 6.0 and 9.5
6.6 - 8.5
-
about half-maximal activity at pH 6.6 and about 90% of maximal activity at pH 8.5, native enzyme
7 - 8.2
-
about 60% of maximal activity at pH 7.0 and about 40% of maximal activity at pH 8.2
7 - 8.2
-
about half-maximal activity at pH 7.0 and 8.2, peak II enzyme
7.1 - 8.3
-
about half-maximal activity at pH 7.1 and 8.3, peak 1 enzyme
7.3 - 9.5
-
about half-maximal activity at pH 7.3 and 9.5
7.5 - 10
-
linear increase up to pH 10 from 10% of maximal activity at pH 7.5
7.8 - 8
-
MgATP-activated enzyme form
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at
25
-
assay at
25
Q9MB58
assay at
25
O64983
assay at
25
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
Q16875
assay at
30
Q52MQ5, Q6PY95
assay at; assay at
30
-
assay at
30
-
assay at
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7 - 4.8
-
isoelectric focusing
9.3
Q52MQ5, Q6PY95
isozymes, sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
equal amounts of isozyme L and M
Manually annotated by BRENDA team
O60825, Q16877
40 human astrocytic gliomas and 20 non-neoplastic brain tissue specimens, different malignity grades, expression analysis in
Manually annotated by BRENDA team
-
low and high malignancy grades according to histological criteria, expression analysis in
Manually annotated by BRENDA team
-
under hypoxia, expression analysis of alternative splice variants in
Manually annotated by BRENDA team
-
expression less detectable in
Manually annotated by BRENDA team
-
two isozymic forms
Manually annotated by BRENDA team
-
2 isozymes: result of alternative splitting of the same primary transcript
Manually annotated by BRENDA team
P70265
transgenic mice, expressed in
Manually annotated by BRENDA team
-
primary culture
Manually annotated by BRENDA team
-
coordinate roles for glucokinase and PFK2 in the elevated hepatic glycolysis in fa/fa rats
Manually annotated by BRENDA team
Q9JJH5
primary culture, treated and untreated with adenoviral vector to overexpress wild-type PFK-2 and mutant PKF2-M lacking Ser-32 phosphorylation site
Manually annotated by BRENDA team
-
resembles muscle enzyme
Manually annotated by BRENDA team
Q7TS91
expressed at high abundance in both hypothalami and clonal hypothalamic neurons. In response to re-feeding, isoform PFKFB3 mRNA levels are increased by 10fold in mouse hypothalami
Manually annotated by BRENDA team
-
engineered to overexpress PFKFB3, inhibitor studies on recombinant PFKFB3 activity in
Manually annotated by BRENDA team
-
placenta-type isozyme is expressed in Kupffer cells of the liver
Manually annotated by BRENDA team
Q75IQ9
mRNA expressed in, metabolite analysis in
Manually annotated by BRENDA team
Q75IQ9
mRNA primarily expressed in, metabolite analysis in
Manually annotated by BRENDA team
-
PFKFB3 is constitutively expressed
Manually annotated by BRENDA team
-
constitutively expressed in
Manually annotated by BRENDA team
-
binding of glucokinase to 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase promotes a coordinated upregulation of glucose phosphorylation and glycolysis in the liver. The interaction may also serve as a metabolic signal transduction pathway for the glucose sensor, glucokinase, in the liver
Manually annotated by BRENDA team
-
sterol regulatory element binding protein-1a binds to a sterol regulatory element box and transcriptionally activates Sparus aurata liver PFKFB1
Manually annotated by BRENDA team
Q16875
transgenic line of Mus musculus
Manually annotated by BRENDA team
-
under hypoxia, expression analysis of alternative splice variants in
Manually annotated by BRENDA team
-
ras-transformed
Manually annotated by BRENDA team
Q7TS91
expressed at high abundance in both hypothalami and clonal hypothalamic neurons
Manually annotated by BRENDA team
O60825, Q16877
expression analysis in
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
low expression in
Manually annotated by BRENDA team
-
under hypoxia, expression analysis of alternative splice variants in
Manually annotated by BRENDA team
additional information
-
tissue distribution, in extrahepatic tissue only 10% or less of activity in liver
Manually annotated by BRENDA team
additional information
-
POROS-HQ column chromatography followed by Western blot analysis of extracts from various rat tissues show that proteins of placenta-type isozyme are expressed in placenta, brain, testis, liver, spleen, heart and lung, but not in kidney and skeletal muscle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
PFKFB3 splice variant 5, the carboxyl terminus is required for this localization
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
-
unfolded monomer, determined by gel filtration
697948
66000
-
native protein, SDS-PAGE
693665
76400
Q52MQ5, Q6PY95
gel filtration
661698
85000 - 90000
-
gel filtration
640282
89100
-
foetal liver, gel filtration
640292
97000
-
gel filtration
640298
98000
-
gel filtration
640310
100000
-
adult liver, gel filtration
640292
100000
-
gel filtration
640295
100000
-
-
640312
101000
-
high speed sedimentation equilibrium
640289
102000
-
gel filtration
640300
107000 - 109000
-
equilibrium sedimentation, sedimentation velocity analysis
94935
110000
-
gel filtration
640300
110000
-
gel filtration
94936
112500
-
gel filtration
640298
118000
-
gel filtration
640303
120000
-
gel filtration
640321
120000
-
gel filtration
94951
132000
-
L-form, gel filtration
640315
140000
Q52MQ5, Q6PY95
recombinant isozyme Tb1, gel filtration
661698
225000
-
gel filtration
640304
250000
-
gel filtration
640320
320000
O64983
gel filtration
640345
370000
Q9MB58
gel filtration
640338
390000
-
H-form, gel filtration
640315
600000
-
gel filtration
94928
additional information
-
amino acid composition
640283, 640289, 640291, 640295
additional information
-
primary structures of human, rat and bovine liver enzyme
640305
additional information
O81398
amino acid composition
94946
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 61000, SDS-PAGE
?
Q52MQ5, Q6PY95
x * 72000, isozyme Tb2, about, sequence calculation, x * 54000, isozyme Tb3, about, sequence calculation, x * 79000, isozyme Tb4, about, sequence calculation
dimer
-
-
dimer
-
2 * 58000, SDS-PAGE
dimer
-
2 * 58000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
2 * 49000, SDS-PAGE
dimer
-
2 * 120000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
active form
dimer
-
2 * 54760, calculated from amino acid sequence
dimer
-
2 * 55800, liver isoenzyme, SDS-PAGE
dimer
-
2 * 55000, high speed sedimentation equilibrium in 6 M guanidinium chloride, amino acid sequence
dimer
-
2 * 53900, muscle-type isozyme, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE, with a minor constituent of MW 54000
dimer
-
2 * 54000, SDS-PAGE, amino acid sequence
dimer
Q52MQ5, Q6PY95
2 * 60000, recombinant Tb1, SDS-PAGE, 2 * 111000, isozyme Tb1, about, sequence calculation
dimer
-
wild-type enzyme in presence of MgATP2-, and C238-pyrene maleimide modified enzyme in presence of beta-D-fructose 6-phosphate and ATP4-
dimer
-
the unfolding pathways of the dimeric (free or fructose-6-phosphate-bound) and tetrameric (MgATP-bound) forms of Pfk-2 are characterized through changes in enzymatic activity and structural properties by intrinsic fluorescence, circular dichroism, 8-anilino-1-naphthalene sulfonic acid binding, gel filtration, and dynamic light scattering measurements
dimer
-
homodimer, oligomerization state necessary for catalysis and stability, presence of MgATP favors the tetrameric form of the enzyme
homodimer
-
determined by circular dichroismand gel filtration, subunits consist of a large domain and an additional beta-sheet that provides the interfacial contacts between the subunits, creating a beta-barrel flattened-like structure with the adjacent subunits beta-sheet, Pfk-2 undergoes a cooperative unfolding/dissociation process with the accumulation of an expanded and unstructured monomeric intermediate with a marginal stability and a large solvent accessibility with respect to the native dimer
tetramer
-
4 * 90000, H-form, SDS-PAGE
tetramer
Q9MB58
4 * 83000
tetramer
O64983
4 * 90800, SDS-PAGE
tetramer
-
inactive form
tetramer
-
wild-type enzyme in absence of ligands, and C238-pyrene maleimide modified enzyme in presence of MgATP2-
tetramer
-
the unfolding pathways of the dimeric (free or fructose-6-hosphate-bound) and tetrameric (MgATP-bound) forms of Pfk-2 are characterized through changes in enzymatic activity and structural properties by intrinsic fluorescence, circular dichroism, 8-anilino-1-naphthalene sulfonic acid binding, gel filtration, and dynamic light scattering measurements
monomer
-
C238-pyrene maleimide modified enzyme in absence of MgATP2-
additional information
-
-
additional information
-
two isozymes: 58000 Da and 54000 Da, SDS-Page
additional information
-
two isozymes: 55000 Da and 52000 Da
additional information
Q52MQ5, Q6PY95
bifunctional enzyme domain structure, the bifunctional enzyme possesses a 6-phosphofructo-2-kinase and a fructose-2,6-bisphosphatase domain, as well as ankyrin-motif repeats, overview
additional information
-
oligomeric state of the enzyme plays a role in enzyme activity and regulation, alterations occur via binding of MgATP2- which mediates dimer-dimer interactions, the dimeric state of the enzyme is critical for stability and activity of the enzyme, Cys-295 plays a role in subunit interactions, overview
additional information
P07953
the enzyme dimer favors binding of monomers in the same Ser32 phosphorylation state in living cells. Phosphorylation at Ser32 may tighten the liver enzyme dimer complex
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase, but no inhibition
phosphoprotein
-
-
phosphoprotein
-
phosphorylation site
phosphoprotein
-
MW 58000 enzyme form
phosphoprotein
-
brain enzyme is phosphorylated, but not activated
phosphoprotein
-
phophorylation by cAMP-dependent protein kinase causes activation
phosphoprotein
-
rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
phosphoprotein
-
phosphorylation by protein kinase C causes activation
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
phosphoprotein
-
rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase, but not rat skeletal muscle, bovine and rat heart enzyme
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation
side-chain modification
-
specific modification by N-(1-pyrenyl)maleimide, the results demonstrate the presence of SH residue in the interface of enzyme subunits critical for interactions between them and that conformational changes occurring through dimers are essential for catalytic activity
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
phosphoprotein
-
-
phosphoprotein
-
phophorylation by cAMP-dependent protein kinase causes activation
phosphoprotein
-
phosphorylation site: Ser-32
phosphoprotein
-
phosphorylation by protein kinase C causes activation
phosphoprotein
Q16875
recombinant His-tagged HBP2, and nontagged wild-type and mutant S460D HBP1 are phosphorylated by several protein kinases, i.e. protein kinases A, B, and C, and by AMP activated kinase, HBP1 mutants are phosphorylated by protein kinase C, overview
phosphoprotein
-
phophorylation by cAMP-dependent protein kinase causes activation, at acid pH-values
phosphoprotein
-
-
phosphoprotein
-
the islet enzyme lacks protein kinase A and C phosphorylation sites
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes 35% inactivation of isozyme L of adipose tissue, not isozyme M
phosphoprotein
-
phophorylation by cAMP-dependent protein kinase causes activation
phosphoprotein
-
phosphorylation site: Ser-32
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not of kidney, testis and heart enzyme
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase of liver enzyme, not of skeletal muscle enzyme, since the phosphorylation site target Ser-32 of the liver isozyme is replaced by Ala in the muscle isozyme
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes 80% decrease in activity of the liver cells but not of hepatoma cells
phosphoprotein
-
phosphorylation at pH 6.6, not at pH 8
phosphoprotein
-
rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase but not rat kidney, testis and skeletal muscle enzyme and bovine and rat heart enzyme
phosphoprotein
-
phosphorylation at lower pH-values
phosphoprotein
-
phosphorylation of foetal liver enzyme by protein kinase C, but no effect on adult liver cells
phosphoprotein
-
loss of phosphorylation-dependent reduction of enzyme by deletion of the N-terminal residues of enzyme, The deletion of 7 N-terminal amino acids causes a 75% decrease in activity
phosphoprotein
-
kinetic of phosphorylation by cAMP-dependent protein kinase
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not of heart and skeletal muscle enzyme
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme
phosphoprotein
-
rat liver enzyme is inhibited by phosphorylation by cAMP-dependent protein kinase, but not rat skeletal muscle, bovine and rat heart enzyme
phosphoprotein
-
the native and the recombinant wild-type and mutant enzymes are phosphorylated after incubation with glucagon inactivating the enzyme
phosphoprotein
Q9JJH5
Ser-32 is the phophorylation site
phosphoprotein
P07953
forskolin induces a 40% increase in phosphorylation at residue Ser32. The enzyme dimer favors binding of monomers in the same Ser32 phosphorylation state in living cells. Phosphorylation at Ser32 may tighten the liver enzyme dimer complex
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase, but no inhibition
phosphoprotein
-
-
phosphoprotein
-
phophorylation by cAMP-dependent protein kinase causes activation
phosphoprotein
-
-
phosphoprotein
-
phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme, not skeletal muscle enzyme
phosphoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour-diffusion method using PEG 6000 as precipitant. Single crystals are grown in the presence of MgATP and diffracted to 1.98 A. The crystals belong to the orthorhombic system, space group P222(1), with unit-cell parameters a = 42.8, b = 86.8, c = 171.3 A
-
oligomeric state observed in the crystal is tetrameric, structural elements involved in the binding of the substrate and allosteric ATPs are also participating in the dimer-dimer interface, data collection parameters and structure refinement statistics
-
His-tagged enzyme recombinantly expressed in Escherichia coli, sitting drop vapor diffusion method
P16118
the crystal structure of liver enzyme: a head-to-head homodimer, depending on the liganding conditions each subunit contains an ATPgammaS, ADP or P molecule to the kinase domain, and two phosphates, regardless of the liganding conditions, bound to phosphatase domain, structure of enzyme very similar to that of the rat testis isoform
-
sitting-drop, vapor-diffusion method, crystal structures of PFKFB3/beta,gamma-methylene-adenosine 5'-triphosphate/fructose-6-phosphate and PFKFB3/ADP/phosphoenolpyruvate complexes are determined to 2.7 A and 2.25 A resolution
-
the crystal structure of H256A to a resolution of 2.4 A by molecular replacement
P25114
the crystal structure of mutant enzyme, the two subunits in the homodimer are arranged in a head-to-head manner, each monomer consists of independent kinase and phosphatase domains, the kinase domains are in close contact, forming an extended hydrophobic core between them, while the phosphatase domains are essentially independent of one another, enzyme is related to the nucleotide monophosphate kinases, and the catalytic domain of G proteins
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
Q9MB58
10 min, enzyme is stable, both in the absence and in the presence of phosphate
640338
25
Q9MB58
about 76% of enzyme activity remains after 10 min, both in the absence and in the presence of phosphate
640338
42
Q9MB58
10 min, activation of enzyme and deletion mutant decreases rapidly, but the presence of phosphate protectes the enzyme activities from inactivation and 75% of enzyme activity remains after 15 min
640338
57
-
10 min, pH 7.1, progressive inactivation, phosphate does not protect
640288
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
very unstable upon purification
-
repeated freeze-thawing inactivates
-
unstable in crude homogenate, iodoacetate, antipain, chymostatin or leupeptin stabilizes, not pepstatin, PMSF or soybean trypsin inhibitor
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, t1/2: 4 h
-
-80C to 0C, at least 1 month
-
-20C, pH 6.8, partially purified, isozyme I, 1 month
-
-80C, partially purified, less than 10% loss of activity within 1 month
-
0C, in 100 mM potassium acetate, 5 mM magnesium acetate, 2.5 mM DTT, 1 mM iodoacetate, 1 mg/ml antipain, 50 mM Tris-acetate, pH 7.8, several h
-
0C, L-form, at least 2 h in the absence of protease inhibitor
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 enzyme forms; heart
-
heart
-
mutant enzyme
-
wild-type and mutant enzyme
-
by Cibacron blue-Sepharose and AMP-agarose chromatography
-
gel filtration
-
recombinant wild-type and mutant enzymes from enzyme-deficient strain DF1020
-
gel filtration, recombinant protein
-
gel filtration; gel filtration; gel filtration; gel filtration
O60825, Q16877
recombinant enzyme
-
recombinant His6-tagged enzyme variants HBP1 and HBP2 and of mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and ion exchange chromatography, the tag is cleaved off, recombinant enzyme form HBP1 partially from Sf9 insect cells by affinity chromatography
Q16875
2 isozymes, liver (L) and muscle (M) type
-
adipose tissue
-
mutant enzyme
-
recombinant enzyme
-
2 isozymes, partial
-
skeletal muscle
-
2 distinct molecular forms; partial
-
multiple molecular forms, predominant: H-(heavy) and L-(light)form
-
recombinant enzymes
O64983
from cytosol, 9000fold by ion exchange and affinity chromatography; native enzyme from stock 427 by ion exchange and affinity chromatography, recombinant His-tagged wild-type and mutant isozyme Tb1 from Escherichia coli
Q52MQ5, Q6PY95
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
generation of transgenic Arabidopsis lines that overexpress both the fructose 6-phosophate 2-kinase and the fructose 2,6-bisphosphatase domain
-
expression in Saccharomyces cerevisiae
Q9MB58
wild-type enzyme, S466E and S466E/S483E mutants are expressed in Escherichia coli BL21(DE3)pLysE and S483E mutant is expressed in BL21(DE3)pLysS, human embryonic kidney 293 cells are transiently transfected with vectors expressing wild-type heart enzyme
-
expressed in Escherichia coli
-
expression of wild-type and mutant enzymes in enzyme-deficient strain DF1020
-
expression in Escherichia coli
-
both parent and double mutant (K472A/K473A) constructs are transformed into the BL21 strain of Escherichia coli, overexpression of PFKFB3 causes no change in glucose metabolism but rather a marked increase in cell proliferation
-
expressed in Escherichia coli, overexpression under the control of the phosphoenolpyruvate carboxykinase promoter in Mus musculus, microinjection of fertilized eggs, C57BL56/SJL receptor females of Mus musculus implanted with microinjected oocytes
Q16875
expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli
O60825, Q16877
isoform of enzyme that is induced by proinflammatory stimuli and that is distinguished by the presence of multiple copies of the AUUUA instability motif in its 3' untranslated region is identified and the complete cDNA is cloned and sequenced, expression in eigth human tumor cell lines
-
mutant expressed in Escherichia coli BL21(DL3)
-
subcloned into the pET-30b(+) vector, expression in BL21 (DE3) Escherichia coli
-
subcloning and overexpression of 2 brain enzyme variants HBP1 and HBP2 and of mutant enzymes as His6-tagged proteins in Escherichia coli, expression of enzyme form HBP1 in Spodoptera frugiperda Sf9 insect cells via baculovirus infection system
Q16875
expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli
A7UAK4, A7UAK5, A7UAK6
expressed in FVB mice, standard embryo microinjection procedures
P70265
using of recombinant testis enzyme
-
expressed in Escherichia coli; expressed in Escherichia coli
Q75IQ9
expression in Escherichia coli
-
expression of wild-type and mutant enzymes in human HEK-293 cells via adenovirus transfection system, overexpression of the mutant enzyme highly increase the endogenous level of glycolysis and fructose 2,6-bisphosphate in presence of glucagon
-
mutant expressed in Escherichia coli BL21(DL3)
-
transfection of RINm5F cell
-
wild-type and mutant protein, expression via adenovirus transfection system in hepatocytes
Q9JJH5
expression in Spodoptera frugiperda cells infected with recombinant baculovirus and Escherichia coli
O64983
DNA and amino acid sequence determination and analysis; DNA and amino acid sequence determination and analysis, phylogenetic analysis of the 6-phosphofructo-2-kinase and the fructose-2,6-bisphosphatase domains, expression of His-tagged wild-type and mutant isozymes Tb1, Tb2, and Tb4 in Escherichia coli, poor expression levels and mostly inactive and unstable isozymes, e.g. recombinant Tb2 is inactive
Q52MQ5, Q6PY95
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ectopic expression of wild type PFKFB3 increases phosphorylation of the cell cycle inhibitor p27, a member of the Kip/Cip family of proteins and a universal inhibitor of cyclin-dependent kinases and the cell cycle, at threonine 187 and decreases total p27 protein levels
-
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 mRNA expression is greater in metastatic prostate cancer compared with primary tumors
Q16877
upon re-feeding, isoform PFKFB3 mRNA levels are increased by 10fold in mouse hypothalami
Q7TS91
maximum expression of Pfkfb3 in cells before puberty, maximum expression of Pfkfb4 in adult cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S466E
-
mutant is phosphorylated by protein kinase B with a stoichiometry to about half that of wild-type enzyme in vitro
S466E/S483E
-
the double mutant is not phosphorylated by protein kinase B, mutation decreases Km of beta-D-fructose 6-phosphate in vitro
S483E
-
mutant is phosphorylated by protein kinase B with a stoichiometry to about half that of wild-type enzyme and mutation decreases citrate inhibition in vitro
C238A
-
site-directed mutagenesis, the mutation does not affect the kinetic parameters, allosteric inhibition, dimer stability, nor oligomeric structure of the enzyme
C238F
-
site-directed mutagenesis, the mutation does not affect the kinetic parameters, allosteric inhibition, dimer stability, nor oligomeric structure of the enzyme
C295A
-
site-directed mutagenesis, decreased kcat and increased Km for ATP and beta-D-fructose 6-phosphate compared to the wild-type enzyme
C295F
-
site-directed mutagenesis, decreased kcat and increased Km for ATP and beta-D-fructose 6-phosphate compared to the wild-type enzyme
E190Q
-
mutant presents a 50fold decrease in the kcat value and a 15fold increment in the apparent Km for MgATP2+. E190Q mutant presents alterations in the inhibition by MgATP2- and phosphate
L307A
-
site-directed mutagenesis, C-terminal point mutant, further mutants analyzed that reveal successive deletions of up to 10 residues at the C-terminal end
R279A
-
mutation eliminates both the binding of ATP to the bisphosphatase domain of the bifunctional enzyme and the activation of enzyme by ATP
R359A
-
mutation eliminates both the binding of ATP to the bisphosphatase domain of the bifunctional enzyme and the activation of enzyme by ATP
H253A
Q16875
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
H253A/S460D
Q16875
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
P2R
-
kinetic properties of human liver mutant and rat wild-type enzyme are very similar
R75A/R76A
-
kinase inactive
S302R
Q16875
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
S460D
Q16875
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
S460D/T470D
Q16875
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
S477D
Q16875
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
T470D
Q16875
site-directed mutagenesis, altered kinetics compared to wild-type enzyme, overview
A44G
-
the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by approximately 20fold compared to wilde-type values
A44V
-
the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by 8fold and 20fold compared to wilde-type values
H256A
P25114
crystal structure
K172A
-
increase in Km of beta-D-fructose 6-phosphate
K172E
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
K172H
-
increase in Km of MgATP2-
K172R
-
increase in Km of beta-D-fructose 6-phosphate
K51A
-
increase in Km of beta-D-fructose 6-phosphate
K51H
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
L148N
-
inactive mutant enzyme
L168A
-
inactive mutant enzyme
P2R
-
kinetic properties of human liver mutant and rat wild-type enzyme are very similar
R136K
-
increase in Km of MgATP2-
R136L
-
increase in Km of beta-D-fructose 6-phosphate
R193H
-
increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate
R193L
-
increase in Km of beta-D-fructose 6-phosphate
R78H
-
increase in Km of MgATP2-
R78L
-
increase in Km of MgATP2-
R79H
-
increase in Km of MgATP2-
R79L
-
increase in Km of MgATP2-
S32A/H258A
-
site-directed mutagenesis, increased activity and incresaed expression level in recombinant HEK-293 cells compared to the wild-type enzyme
S32A/H258A
P07953
mutant unable to be phosphorylated
additional information
Q9MB58
the deletion of N-terminal 318 amino acids abolishes the Michaelis-Menten kinetics of enzyme, Km of beta-D-fructose 6-phosphate is increased, whereas Km of ATP is not significantly altered. When the first 66 amino acids are deleted, the activity ration between 6-phosphofructo-2-kinase and beta-D-fructose 2,6-bisphosphatase is halved. The deletion of 125, 179, 249 and 318 amino acids results in progressive further decreases in the activity ratio and the activity ratio is reduced 4fold when N-terminus is deleted completely. The full-length enzyme is eluted as a tetramer, whereas the truncated enzymes are eluted as monomers
additional information
-
mutant enzymes of rat testis are constructed, in which its terminal peptides are replaced with those of the liver or the heart enzyme
Y306A
-
site-directed mutagenesis, C-terminal point mutant, no dimer-tetramer conversion in presence of MgATP, inhibition pattern almost undistinguishable from the wild-type, conformational changes leading to allosteric inhibition can be uncoupled from tetramer formation at least in the Y306A mutant
additional information
-
the chicken enzyme in which the C-termini tail were replaced with that of rat enzyme is not activated by ATP, a series of C-terminal deletion mutants are generated: 15, 20, 25 and 30 amino acids, the deletion of the C-terminal 25 or 30 residues of enzyme increases Km of beta-D-fructose 6-phosphate by approximately 2fold. The mutations E446A, H444A, H444K, H444E, R445E, R445L prove the importance of His444 and Arg445.The C-terminal region I involves in the activation of enzyme by ATP.
K472A/K473A
-
cytoplasmic mutant
additional information
Q16875
construction of a chimeric mutant fusing the N-terminal portion of residues 1-444 of the human enzyme to the C-terminal part, residues 450-530, of the Bos taurus enzyme, i.e. HBPBHP, construction of a deletion mutant lacking the entire carboxyterminal region of residues 446-519
L168R
-
mutant enzyme shows 0.2% of wild-type activity
additional information
-
-
additional information
-
effects of N- and C-terminal deletions of skeletal muscle and liver enzyme, e.g. ND4, ND7, ND12, ND23, CD30, comparison of the kinetic properties of deletion mutants
additional information
-
mutant enzymes of rat testis are constructed, in which its terminal peptides are replaced with those of the liver or the heart enzyme
additional information
-
ATP binding and the effect of pH on the kinetics are characterized
additional information
-
mutant enzyme, in which the four tryptophan residues in the isoenzyme are mutated to phenylalanine, structure
additional information
-
enzyme contains four tryptophan residues: Trp15, Trp64, Trp299 and Trp320, mutant enzymes contain either no Trp or a single Trp at each location, the other Trp residues having been converted to Phe, mutations do not cause large change in protein conformation and function, Trp299 and Trp320 in mutant enzymes quenched by iodide to a small extent can indicate an altered conformation, Trp64 is not accessible
additional information
-
engineering of the LKVWT glucokinase-binding motif in the FBPase-2 domain of islet PFK-2/FBPase-2 to HKEWR leads to significantly lower interaction with glucokinase compared with wild-type at 25 mmol/liter glucose
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
for refolding experiments, the enzyme is first exposed to 3 M GdnHCl for 5 h at 20C, under this condition Pfk-2 is completely unfolded, the refolding curve is obtained diluting the unfolded enzyme to several guanidine hydrochloride concentrations in the 50 mM Tris, pH 7.8, 5 mM MgCl2 and 10 mM dithiotreitol, under these conditions equilibrium is achieved after 5 h of incubation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
P16118
a molecule in which EDTA is covalently linked to ADP is a good starting molecule for the development of new cancer-therapeutic molecules
medicine
-
the key role of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in neoplastic transformation provides a rational for the development of agents that selectively inhibit the PFKFB3 enzyme as antineoplastic agents
medicine
-
the pharmacologic inhibition of this enzyme may effect the survival and growth of neoplastic cells
medicine
-
clinical development of PFKFB3 inhibitors as chemotherapeutic agents
medicine
Q16877
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 mRNA expression is greater in metastatic prostate cancer compared with primary tumors
pharmacology
O60825, Q16877
role of PFKFB3 protein in tumorigenesis, expression studies in human astrocytic gliomas of different malignancy grades
medicine
-
the pharmacologic inhibition of this enzyme may effect the survival and growth of neoplastic cells
medicine
P70265
analysis of increase in cardiac glycolysis during ischemia and heart failure
pharmacology
Q9JJH5
effects of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR) on hepatic glucose metabolism