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Information on EC 2.7.1.146 - ADP-specific phosphofructokinase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58999

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IUBMB Comments
ADP can be replaced by GDP, ATP and GTP, to a limited extent. Divalent cations are necessary for activity, with Mg2+ followed by Co2+ being the most effective.
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Methanocaldococcus jannaschii
UNIPROT: Q58999
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
adp-dependent phosphofructokinase, tlpfk, tk0376, adp-dependent 6-phosphofructokinase, adp-dependent pfk, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADP dependent phosphofructokinase
-
-
-
-
ADP-6-phosphofructokinase
-
-
-
-
ADP-dependent glucokinase/phosphofructokinase
-
bifunctional enzyme
ADP-dependent phosphofructokinase
-
-
-
-
ADP-Pfk
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-
-
-
additional information
see also EC 2.7.1.147
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ADP:D-fructose-6-phosphate 1-phosphotransferase
ADP can be replaced by GDP, ATP and GTP, to a limited extent. Divalent cations are necessary for activity, with Mg2+ followed by Co2+ being the most effective.
CAS REGISTRY NUMBER
COMMENTARY hide
237739-62-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-phosphate + D-fructose 6-phosphate
acetate + D-fructose 1,6-bisphosphate
show the reaction diagram
activity is 83% compared to the activity with ADP
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
show the reaction diagram
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
show the reaction diagram
additional information
?
-
the enzyme from Methanococcus jannaschii also shows glucokinase activity, a bifunctional MjPFK/GK
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-
-
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
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
show the reaction diagram
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
activity is highest in the presence of CaCl2, followed by MgCl2, Co2+ and Mn2+
Co2+
activity is highest in the presence of CaCl2, followed by MgCl2, Co2+ and Mn2+
Mn2+
activity is highest in the presence of CaCl2, followed by MgCl2, Co2+ and Mn2+
Mn2+
-
40% of activity
Ni2+
-
40% of activity
Pb2+
-
40% of activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
10 mM, 76% inhibition
ATP
10 mM, 47% inhibition
KCl
500 mM, 16% inhibition
NaCl
500 mM, 12% inhibition
Zn2+
no activity detected in presence of Zn2+
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.9
acetyl-phosphate
pH 6.5, 50°C
0.0063 - 0.0096
D-fructose 6-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.7
D-fructose 6-phosphate
pH 6.5, 40°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
428.6
D-fructose 6-phosphate
pH 6.5, 40°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2
pH 6.5, 50°C, direction of phosphorylation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
physiological function
key enzyme of the modified Embden-Meyerhof pathway of heterotrophic and chemolithoautotrophic archaea
additional information
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50100
non-denaturing PAGE
53362
1 * 53362, calculated from sequence
53000
-
1 * 53000, SDS-PAGE
55000
-
high pressure liquid chromatography
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 53362, calculated from sequence
monomer
-
1 * 53000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene pfkC, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sakuraba, H.; Yoshioka, I.; Koga, S.; Takahashi, M.; Kitahama, Y.; Satomura, T.; Kawakami, R.; Ohshima, T.
ADP-dependent glucokinase/phosphofructokinase, a novel bifunctional enzyme from the hyperthermophilic archaeon Methanococcus jannaschii
J. Biol. Chem.
277
12495-12498
2002
Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Verhees, C.H.; Tuininga, J.E.; Kengen, S.W.; Stams, A.J.; van der Oost, J.; de Vos, W.M.
ADP-dependent phosphofructokinases in mesophilic and thermophilic methanogenic archaea
J. Bacteriol.
183
7145-7153
2001
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii (Q58999), Methanocaldococcus jannaschii DSM 2661 (Q58999)
Manually annotated by BRENDA team
Merino, F.; Guixe, V.
Specificity evolution of the ADP-dependent sugar kinase family: in silico studies of the glucokinase/phosphofructokinase bifunctional enzyme from Methanocaldococcus jannaschii
FEBS J.
275
4033-4044
2008
Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Castro-Fernandez, V.; Herrera-Morande, A.; Zamora, R.; Merino, F.; Gonzalez-Ordenes, F.; Padilla-Salinas, F.; Pereira, H.M.; Brandao-Neto, J.; Garratt, R.C.; Guixe, V.
Reconstructed ancestral enzymes reveal that negative selection drove the evolution of substrate specificity in ADP-dependent kinases
J. Biol. Chem.
292
15598-15610
2017
Methanocaldococcus jannaschii (Q58999), Pyrococcus horikoshii (O59355), Pyrococcus horikoshii ATCC 700860 (O59355), uncultured bacterium
Manually annotated by BRENDA team