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Information on EC 2.7.1.11 - 6-phosphofructokinase and Organism(s) Geobacillus stearothermophilus and UniProt Accession P00512

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EC Tree
IUBMB Comments
The enzyme from rabbit muscle displays absolute stereoselectivity for the beta-anomer of D-fructofuranose 6-phosphate [9-11]. D-Tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. UTP, CTP and ITP can act as donors. Not identical with EC 2.7.1.105 6-phosphofructo-2-kinase.
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This record set is specific for:
Geobacillus stearothermophilus
UNIPROT: P00512
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Word Map
The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
phosphofructokinase, 6-phosphofructokinase, 6-phosphofructo-1-kinase, pfk-1, phosphofructokinase-1, pfk-m, phosphofructokinase 1, atp-dependent phosphofructokinase, atp-pfk, pfk-l, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphofructokinase-1
-
6-phosphofructokinase, platelet type
-
-
-
-
6-phosphofructose 1-kinase
-
-
-
-
6-phosphofructose-1-kinase
-
-
-
-
ATP-dependent phosphofructokinase
-
-
-
-
ATP-PFK
-
-
-
-
D-fructose-6-phosphate 1-phosphotransferase
-
-
-
-
fructose 6-phosphate kinase
-
-
-
-
fructose 6-phosphokinase
-
-
-
-
kinase, phosphofructo- (phosphorylating)
-
-
-
-
nucleotide triphosphate-dependent phosphofructokinase
-
-
-
-
PFK
-
-
-
-
PFK1
-
-
-
-
PFK2
-
-
-
-
phospho-1,6-fructokinase
-
-
-
-
phosphofructokinase
-
-
-
-
phosphofructokinase 1
-
-
-
-
phosphohexokinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + beta-D-fructofuranose 6-phosphate = ADP + beta-D-fructofuranose 1,6-bisphosphate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-fructose-6-phosphate 1-phosphotransferase
The enzyme from rabbit muscle displays absolute stereoselectivity for the beta-anomer of D-fructofuranose 6-phosphate [9-11]. D-Tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. UTP, CTP and ITP can act as donors. Not identical with EC 2.7.1.105 6-phosphofructo-2-kinase.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-80-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
CTP + D-fructose 6-phosphate
CDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
GTP + D-fructose 6-phosphate
GDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
UTP + D-fructose 6-phosphate
UDP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
contains Ca2+ ions
Mg2+
-
required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphoenolpyruvate
I153V mutation has a substantial positive impact on the magnitude of inhibition by phosphoenolpyruvate
additional information
-
product inhibition of reverse reaction
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GDP
-
activation at low concetrations, inhibition above 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
100 - 129
D-fructose 6-phosphate
0.07 - 0.13
ATP
2.6
CTP
-
pH 8.2, 30°C
0.023 - 0.15
D-fructose 6-phosphate
0.18
GTP
-
pH 8.2, 30°C
2.8
UTP
-
pH 8.2, 30°C
additional information
additional information
-
kinetic study
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.2
fructose 1,6-bisphosphate
-
reverse raction, recombinant enzyme
112 - 149
fructose 6-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PFKA_GEOSE
319
0
34119
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.2 M calcium acetate hydrate, 0.1 M sodium cacodylate trihydrate pH 6.5, and 18% (w/v) polyethylene glycol 8000, at 16°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I150V
Km-value for D-fructose 6-phosphate is 1.1fold lower than the wild-type value
I153V
mutation has a substantial positive impact on the magnitude of inhibition by phosphoenolpyruvate
I234V
Km-value for D-fructose 6-phosphate is comparable to the wild-type value
G212V
K90/91E
-
surface charge-tag substitution, no change in Km for ATP and K1/2 for fructose 6-phosphate
R162E
-
single active site substitution, affinity for fructose 6-phosphate is diminished approx. 3 orders of magnitude relative to that of the wild-type
R211E/K213E
-
allosteric site substitutions
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 100 mM Tris-HCl buffer, pH 7.4, 1 mM dithiothreitol, 50% glycerol, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Mimetic Blue 1 column chromatography and Mono Q column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli RL257 cells
expression in Escherichia coli
-
expression of wild-type and G212V mutant PFK in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Byrnes, M.; Zhu, X.; Younathan, E.S.; Chang, S.H.
Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme
Biochemistry
33
3424-3431
1994
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Shirakihara, Y.; Evans, P.R.
Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products
J. Mol. Biol.
204
973-994
1988
Geobacillus stearothermophilus, Escherichia coli, Escherichia coli DF1020
Manually annotated by BRENDA team
Zhu, X.; Byrnes, M.; Nelson, J.W.; Chang, S.H.
Role of glycine 212 in the allosteric behavior of phosphofructokinase from Bacillus stearothermophilus
Biochemistry
34
2560-2565
1995
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Kimmel, J.L.; Reinhart, G.D.
Isolation of an individual allosteric interaction in tetrameric phosphofructokinase from Bacillus stearothermophilus
Biochemistry
40
11623-11629
2001
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Mosser, R.; Reddy, M.; Bruning, J.; Sacchettini, J.; Reinhart, G.
Structure of the apo form of Bacillus stearothermophilus phosphofructokinase
Biochemistry
51
769-775
2012
Geobacillus stearothermophilus (P00512), Geobacillus stearothermophilus
Manually annotated by BRENDA team
Whitaker, A.; Reinhart, G.
The effect of introducing small cavities on the allosteric inhibition of phosphofructokinase from Bacillus stearothermophilus
Arch. Biochem. Biophys.
607
1-6
2016
Geobacillus stearothermophilus (P00512), Geobacillus stearothermophilus
Manually annotated by BRENDA team