BRENDA - Enzyme Database
show all sequences of 2.7.1.146

ADP-dependent 6-phosphofructokinase, an extremely thermophilic, non-allosteric enzyme from the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324

Hansen, T.; Schonheit, P.; Extremophiles 8, 29-35 (2004)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
no allosterical regulation by ADP, AMP, phosphoenolpyruvate, or citrate
Archaeoglobus fulgidus
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
no allosterical regulation by ADP, AMP, phosphoenolpyruvate, or citrate
Archaeoglobus fulgidus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.3
-
ADP
pH 6.6, 50°C
Archaeoglobus fulgidus
0.6
-
ADP
pH 6.6, 80°C
Archaeoglobus fulgidus
1.4
-
AMP
pH 6.6, 80°C
Archaeoglobus fulgidus
2.2
-
D-fructose 6-phosphate
pH 6.6, 80°C
Archaeoglobus fulgidus
4.7
-
D-fructose 6-phosphate
pH 6.6, 50°C
Archaeoglobus fulgidus
5.7
-
D-fructose 1,6-bisphosphate
pH 6.6, 80°C
Archaeoglobus fulgidus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Archaeoglobus fulgidus
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
30% of activity with Mg2+
Archaeoglobus fulgidus
Fe2+
16% of activity with Mg2+
Archaeoglobus fulgidus
Mg2+
most efficient divalent cation, can be replaced by Ni2+, Co2+, and Mn2+
Archaeoglobus fulgidus
Mn2+
62% of activity with Mg2+
Archaeoglobus fulgidus
additional information
divalent cations are required for activity, Zn2+, Ca2+, and Cu2+ are poor metal cofactors
Archaeoglobus fulgidus
Ni2+
33% of activity with Mg2+
Archaeoglobus fulgidus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
2 * 50000, SDS-PAGE; 4 * 50000, SDS-PAGE
Archaeoglobus fulgidus
100000
-
dimeric enzyme form, gel filtration at higher protein concentration
Archaeoglobus fulgidus
200000
-
tetrameric enzyme form, gel filtration at lower protein concentration
Archaeoglobus fulgidus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ADP + D-fructose 6-phosphate
Archaeoglobus fulgidus
-
AMP + D-fructose 1,6-bisphosphate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Archaeoglobus fulgidus
-
strain 7324, no activity in strain VC 16
-
Purification (Commentary)
Commentary
Organism
1818fold to homogeneity by ultracentrifugation, anion exchange, ADP affinity, and cation exchange chromatography, and gel filtration
Archaeoglobus fulgidus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
12
-
purified enzyme, determined at pH 6.6, 80°C, reverse reaction
Archaeoglobus fulgidus
392
-
purified enzyme, determined at pH 6.6, 50°C, forward reaction
Archaeoglobus fulgidus
Storage Stability
Storage Stability
Organism
-20°C, purified native enzyme, quite stable
Archaeoglobus fulgidus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP + D-fructose 6-phosphate
-
661677
Archaeoglobus fulgidus
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
ADP + D-fructose 6-phosphate
enzyme is highly specific for D-fructose 6-phosphate in the forward reaction
661677
Archaeoglobus fulgidus
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
additional information
no activity with ATP, diphosphate, or acetyl phosphate as phosphate donors, no activity with D-glucose as phosphate acceptor substrate
661677
Archaeoglobus fulgidus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 * 50000, SDS-PAGE
Archaeoglobus fulgidus
tetramer
4 * 50000, SDS-PAGE
Archaeoglobus fulgidus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
-
Archaeoglobus fulgidus
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
40
100
-
Archaeoglobus fulgidus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
80
-
120 min, completely stable
Archaeoglobus fulgidus
100
-
120 min, completely loss of activity after 60 min, in presence of 1 M NaCl the enzyme retains 30% activity after 90 min, in presence of 1 M KCl the enzyme retains 50% activity after 90 min
Archaeoglobus fulgidus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.6
-
-
Archaeoglobus fulgidus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
3.9
9
50% of maximal activity at pH 6.1 and pH 7.9
Archaeoglobus fulgidus
Cofactor
Cofactor
Commentary
Organism
Structure
ADP
-
Archaeoglobus fulgidus
additional information
no activity with ATP, diphosphate, or acetyl phosphate
Archaeoglobus fulgidus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
no allosterical regulation by ADP, AMP, phosphoenolpyruvate, or citrate
Archaeoglobus fulgidus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ADP
-
Archaeoglobus fulgidus
additional information
no activity with ATP, diphosphate, or acetyl phosphate
Archaeoglobus fulgidus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
no allosterical regulation by ADP, AMP, phosphoenolpyruvate, or citrate
Archaeoglobus fulgidus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.3
-
ADP
pH 6.6, 50°C
Archaeoglobus fulgidus
0.6
-
ADP
pH 6.6, 80°C
Archaeoglobus fulgidus
1.4
-
AMP
pH 6.6, 80°C
Archaeoglobus fulgidus
2.2
-
D-fructose 6-phosphate
pH 6.6, 80°C
Archaeoglobus fulgidus
4.7
-
D-fructose 6-phosphate
pH 6.6, 50°C
Archaeoglobus fulgidus
5.7
-
D-fructose 1,6-bisphosphate
pH 6.6, 80°C
Archaeoglobus fulgidus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Archaeoglobus fulgidus
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
30% of activity with Mg2+
Archaeoglobus fulgidus
Fe2+
16% of activity with Mg2+
Archaeoglobus fulgidus
Mg2+
most efficient divalent cation, can be replaced by Ni2+, Co2+, and Mn2+
Archaeoglobus fulgidus
Mn2+
62% of activity with Mg2+
Archaeoglobus fulgidus
additional information
divalent cations are required for activity, Zn2+, Ca2+, and Cu2+ are poor metal cofactors
Archaeoglobus fulgidus
Ni2+
33% of activity with Mg2+
Archaeoglobus fulgidus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
2 * 50000, SDS-PAGE; 4 * 50000, SDS-PAGE
Archaeoglobus fulgidus
100000
-
dimeric enzyme form, gel filtration at higher protein concentration
Archaeoglobus fulgidus
200000
-
tetrameric enzyme form, gel filtration at lower protein concentration
Archaeoglobus fulgidus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ADP + D-fructose 6-phosphate
Archaeoglobus fulgidus
-
AMP + D-fructose 1,6-bisphosphate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
1818fold to homogeneity by ultracentrifugation, anion exchange, ADP affinity, and cation exchange chromatography, and gel filtration
Archaeoglobus fulgidus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
12
-
purified enzyme, determined at pH 6.6, 80°C, reverse reaction
Archaeoglobus fulgidus
392
-
purified enzyme, determined at pH 6.6, 50°C, forward reaction
Archaeoglobus fulgidus
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, purified native enzyme, quite stable
Archaeoglobus fulgidus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP + D-fructose 6-phosphate
-
661677
Archaeoglobus fulgidus
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
ADP + D-fructose 6-phosphate
enzyme is highly specific for D-fructose 6-phosphate in the forward reaction
661677
Archaeoglobus fulgidus
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
additional information
no activity with ATP, diphosphate, or acetyl phosphate as phosphate donors, no activity with D-glucose as phosphate acceptor substrate
661677
Archaeoglobus fulgidus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 50000, SDS-PAGE
Archaeoglobus fulgidus
tetramer
4 * 50000, SDS-PAGE
Archaeoglobus fulgidus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
-
Archaeoglobus fulgidus
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
40
100
-
Archaeoglobus fulgidus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
80
-
120 min, completely stable
Archaeoglobus fulgidus
100
-
120 min, completely loss of activity after 60 min, in presence of 1 M NaCl the enzyme retains 30% activity after 90 min, in presence of 1 M KCl the enzyme retains 50% activity after 90 min
Archaeoglobus fulgidus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.6
-
-
Archaeoglobus fulgidus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
3.9
9
50% of maximal activity at pH 6.1 and pH 7.9
Archaeoglobus fulgidus
Other publictions for EC 2.7.1.146
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
727486
Castro-Fernandez
Bifunctional ADP-dependent pho ...
Methanococcus maripaludis
FEBS J.
281
2017-2029
2014
1
-
1
1
-
-
6
6
-
5
-
2
-
1
-
-
1
-
-
-
-
-
11
-
-
-
-
5
2
2
-
-
4
-
4
1
-
1
-
1
-
-
4
6
4
6
-
5
-
2
-
-
-
1
-
-
-
-
11
-
-
-
-
5
2
2
-
-
-
-
-
-
6
6
721764
Merino
Catalytic and regulatory roles ...
Pyrococcus horikoshii
Biochimie
94
516-524
2012
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
3
3
698924
Currie
ADP-dependent 6-phosphofructok ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
J. Biol. Chem.
284
22664-22671
2009
-
-
1
1
15
-
3
30
-
7
-
1
-
6
-
-
1
-
-
-
-
-
11
-
1
-
-
16
-
-
-
5
-
-
-
-
-
2
6
2
29
-
-
3
-
58
-
7
-
1
-
-
-
2
-
-
-
-
11
-
1
-
-
30
-
-
-
-
-
1
1
-
30
30
686707
Merino
Specificity evolution of the A ...
Methanocaldococcus jannaschii
FEBS J.
275
4033-4044
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
661677
Hansen
ADP-dependent 6-phosphofructok ...
Archaeoglobus fulgidus
Extremophiles
8
29-35
2004
1
-
-
-
-
-
1
6
1
6
3
1
-
4
-
-
1
-
-
-
2
1
3
2
1
1
2
-
1
1
-
2
-
-
-
1
-
-
2
-
-
-
-
1
-
6
1
6
3
1
-
-
-
1
-
-
2
1
3
2
1
1
2
-
1
1
-
-
-
-
-
-
-
-
660573
Jeong
Archaeal ADP-dependent phospho ...
Thermococcus litoralis
Acta Crystallogr. Sect. D
59
1327-1329
2003
-
-
1
1
-
-
-
1
-
1
2
1
-
3
-
-
1
-
-
-
1
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
-
-
-
-
-
1
-
1
2
1
-
-
-
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
395244
Sakuraba
ADP-dependent glucokinase/phos ...
Methanocaldococcus jannaschii
J. Biol. Chem.
277
12495-12498
2002
-
-
1
-
-
-
-
-
-
6
2
1
-
5
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
6
2
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
395242
Kengen
ADP-dependent glucokinase and ...
Pyrococcus furiosus
Methods Enzymol.
331
41-53
2001
-
-
1
-
-
-
2
-
-
2
2
1
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
-
2
2
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
395269
Verhees
ADP-dependent phosphofructokin ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
J. Bacteriol.
183
7145-7153
2001
-
-
1
-
-
-
6
3
-
4
2
4
-
13
-
-
1
-
-
-
1
-
8
1
1
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
6
-
3
-
6
3
4
-
-
-
2
-
-
2
-
8
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
395270
Ronimus
Sequencing, expression, charac ...
Thermococcus zilligii
Biochim. Biophys. Acta
1517
384-391
2001
-
-
1
-
-
-
-
-
-
-
3
1
-
7
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
3
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
721449
Labes
Sugar utilization in the hyper ...
Archaeoglobus fulgidus, Archaeoglobus fulgidus 7324
Arch. Microbiol.
176
329-338
2001
-
-
-
-
-
-
-
2
-
-
-
1
-
9
-
-
-
-
-
2
2
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
2
2
-
2
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
395266
Tuininga
Molecular and biochemical char ...
Pyrococcus furiosus
J. Biol. Chem.
274
21023-21028
1999
-
-
1
-
-
-
2
-
-
2
2
1
-
4
-
-
1
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
-
2
2
1
-
-
-
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
395267
Ronimus
Purification and characterizat ...
Thermococcus zilligii
Extremophiles
3
121-129
1999
-
-
-
-
-
-
-
-
-
3
2
1
-
2
-
-
1
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
2
1
-
-
-
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722596
Kengen
Evidence for the operation of ...
Pyrococcus furiosus
J. Biol. Chem.
269
17537-17541
1994
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
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