BRENDA - Enzyme Database
show all sequences of 2.7.1.146

Bifunctional ADP-dependent phosphofructokinase/glucokinase activity in the order Methanococcales - biochemical characterization of the mesophilic enzyme from Methanococcus maripaludis

Castro-Fernandez, V.; Bravo-Moraga, F.; Herrera-Morande, A.; Guixe, V.; FEBS J. 281, 2017-2029 (2014)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
D-glucosamine
10 mM, 40% activation of glucokinase activity
Methanococcus maripaludis
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Methanococcus maripaludis
Crystallization (Commentary)
Crystallization
Organism
molecular modeling of structure. for binding of ADP, residues M347, I431 and L441 create a hydrophobic pocket around the adenine group. R194 makes a hydrogen bond with alpha and beta phosphates, carbonyl and NH groups from V432 peptide bond make a hydrogen bond with the NH2 group of C6 and the N1 atom of adenine
Methanococcus maripaludis
Inhibitors
Inhibitors
Commentary
Organism
Structure
ADP
; strong inhibition effect in the reverse glucokinase reaction
Methanococcus maripaludis
AMP
strong substrate inhibition effect in the reverse glucokinase reaction
Methanococcus maripaludis
D-fructose
-
Methanococcus maripaludis
D-fructose 6-phosphate
; strong inhibition of glucokinase activity, competitive inhibion versus D-glucose as variable substrate
Methanococcus maripaludis
D-glucose
; substrate inhibition above 200 mM. At 10 mM 20% inhibition of phosphofructokinase activity
Methanococcus maripaludis
EDTA
50 mM, complete inhibition; complete loss of activity; completely abolishes activity
Methanococcus maripaludis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.065
-
D-fructose 6-phosphate
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
0.1
2
D-fructose 1,6-bisphosphate
pH 6.5, 30°C
Methanococcus maripaludis
0.1
2
D-glucose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
0.12
-
D-fructose 1,6-bisphosphate
pH 7.0, 30°C
Methanococcus maripaludis
8
-
ADP
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
40
-
D-glucose
pH 6.5, 30°C
Methanococcus maripaludis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
2 mM, about 70% of the activity with Mg2+; 2 mM, divalent metal ion required, activation of phosphofructokinase activity with Co2+ is about 70% compared to the activation with Mg2+, activation of glucokinase activity is about 35% compared to the activation with Mg2+; among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured
Methanococcus maripaludis
Mg2+
2 mM, divalent metal ion required, highest activity is observed in the presence of Mg2+; among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured; highest activity in the presence of Mg2+
Methanococcus maripaludis
Mn2+
2 mM, about 25% of the activity with Mg2+; 2 mM, divalent metal ion required, activation of phosphofructokinase activity with Co2+ is about 25% compared to the activation with Mg2+, activation of glucokinase activity is about 20% compared to the activation with Mg2+; among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured
Methanococcus maripaludis
additional information
divalent cation required, with highest activity in the presence of Mg2+
Methanococcus maripaludis
Ni2+
2 mM, divalent metal ion required, activation of phosphofructokinase activity with Co2+ is about 30% compared to the activation with Mg2+, activation of glucokinase activity is less than 10% compared to the activation with Mg2+; among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured
Methanococcus maripaludis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ADP + D-fructose 6-phosphate
Methanococcus maripaludis
-
AMP + D-fructose 1,6-bisphosphate
-
-
ir
ADP + D-glucose
Methanococcus maripaludis
the enzyme phosphorylates both D-glucose and D-fructose 6-phosphate. Binding of both substrates to the same active site. At a sugar concentration of 10 mM the acctivity with D-fructose 6-phosphate is about 75% compared to the activity with D-glucose. No activity in presence of ATP. kcat/KM for the phosphorylation of D-fructose 6-phosphate is 440fold higher than the kcat/Km for the phosphorylation of glucose. Analysis of the kcat/Km ratios shows that the glucose dephosphorylation is 2fold more effective than the phosphorylation
AMP + D-glucose 6-phosphate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanococcus maripaludis
Q6LXQ3
; bifunctional ADP-dependent phosphofructokinase/glucokinase, reactions of EC 2.7.1.147 and EC 2.7.1.146, respectively
-
Purification (Commentary)
Commentary
Organism
-
Methanococcus maripaludis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ADP + D-fructose 6-phosphate
-
727486
Methanococcus maripaludis
AMP + D-fructose 1,6-bisphosphate
-
-
-
ir
ADP + D-fructose 6-phosphate
the bifunctional enzyme is able to phosphorylate D-glucose and beta-D-fructose 6-phosphate. The results of molecular modeling show that both sugars are bound to the enzyme by essentially the same residues except for N203, which establishes an interaction only when the substrate is D-fructose 6-phosphate, and E79, which interacts only with glucose. The enzyme shows higher activity with glucose compared to that obtained with beta-D-fructose 6-phosphate. beta-D-Fructose 6-phosphate shows 75% of the activity measured with glucose. In the presence of ATP, no activity is detected. Phosphatase activity is 67-fold lower than the kinase activity
727486
Methanococcus maripaludis
AMP + D-fructose 1,6-bisphosphate
-
-
-
ir
ADP + D-fructose 6-phosphate
the enzyme phosphorylates both D-glucose and D-fructose 6-phosphate. Binding of both substrates to the same active site. At a sugar concentration of 10 mM the activity with D-fructose 6-phosphate is about 75% compared to the activity with D-glucose. No activity in presence of ATP. kcat/KM for the phosphorylation of D-fructose 6-phosphate is 440fold higher than the kcat/Km for the phosphorylation of glucose
727486
Methanococcus maripaludis
AMP + D-fructose 1,6-bisphosphate
-
-
-
ir
ADP + D-fructose 6-phosphate
kinetics show hyperbolic behavior
727486
Methanococcus maripaludis
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
ADP + D-glucose
the enzyme phosphorylates both D-glucose and D-fructose 6-phosphate. Binding of both substrates to the same active site. At a sugar concentration of 10 mM the acctivity with D-fructose 6-phosphate is about 75% compared to the activity with D-glucose. No activity in presence of ATP. kcat/KM for the phosphorylation of D-fructose 6-phosphate is 440fold higher than the kcat/Km for the phosphorylation of glucose. Analysis of the kcat/Km ratios shows that the glucose dephosphorylation is 2fold more effective than the phosphorylation
727486
Methanococcus maripaludis
AMP + D-glucose 6-phosphate
-
-
-
r
ADP + D-glucose
the enzyme phosphorylates both D-glucose and D-fructose 6-phosphate.Binding of both substrates to the same active site. At a sugar concentration of 10 mM the acctivity with D-fructose 6-phosphate is about 75% compared to the activity with D-glucose. No activity in presence of ATP. kcat/KM for the phosphorylation of D-fructose 6-phosphate is 440fold higher than the kcat/Km for the phosphorylation of glucose. Analysis of the kcat/Km ratios shows that the glucose dephosphorylation is 2fold more effective than the phosphorylation
727486
Methanococcus maripaludis
AMP + D-glucose 6-phosphate
-
-
-
r
AMP + D-fructose 1,6-bisphosphate
-
727486
Methanococcus maripaludis
ADP + D-fructose 6-phosphate
-
-
-
r
CDP + beta-D-fructose 6-phosphate
about 15% compared to the activity with ADP
727486
Methanococcus maripaludis
CMP + D-fructose 1,6-bisphosphate
-
-
-
ir
additional information
less than 10% activity compared to the activity with D-glucose and ADP: L-rhamnose, D-arabinose, D-lyxose, D-fucose, D-galactose, D-mannose, D-fructose, 2-deoxyglucose, D-glucosamine, D-xylose, maltose, lactose
727486
Methanococcus maripaludis
?
-
-
-
-
additional information
bifunctional ADP-dependent phosphofructokinase/glucokinase, reactions of EC 2.7.1.147 and EC 2.7.1.146, respectively. The rate at which fructose 6-phosphate is phosphorylated is 440fold higher than the glucose phosphorylation rate
727486
Methanococcus maripaludis
?
-
-
-
-
UDP + D-glucose
the enzyme phosphorylates both D-glucose and D-fructose 6-phosphate. Activity with UDP and D-glucose is about 20% compared to the activity with ADP and D-glucose
727486
Methanococcus maripaludis
UMP + D-glucose 6-phosphate
-
-
-
r
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.45
-
D-fructose 1,6-bisphosphate
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
0.45
-
D-glucose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
16.5
-
D-fructose 6-phosphate
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
23
-
D-glucose
pH 6.5, 30°C
Methanococcus maripaludis
30
-
ADP
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
; phosphofructokinase activity
Methanococcus maripaludis
7
-
; glucokinase activity
Methanococcus maripaludis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
7
pH 5.0: about 50% of maximal activity, pH 7.0: about 65% of maximal activity; pH 5.0: about 50% of maximal phosphofructokinase activity, pH 7.0: about 65% of maximal phosphofructokinase activity
Methanococcus maripaludis
5.5
7.5
pH 5.5: about 50% of maximal phosphofructokinase activity, pH 7.5: about 75% of maximal phosphofructokinase activity
Methanococcus maripaludis
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.226
-
D-fructose 6-phosphate
pH 7.5, 30°C, glucokinase reaction
Methanococcus maripaludis
0.4
-
AMP
pH 7.5, 30°C, reverse glucokinase reaction
Methanococcus maripaludis
54
-
ADP
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
895
-
D-glucose
pH 7.5, 30°C
Methanococcus maripaludis
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.08
-
pH 7.5, 30°C, reverse glucokinase reaction
Methanococcus maripaludis
ADP
0.22
-
pH 6.5, 30°C; pH 7.5, 30°C, glucokinase reaction
Methanococcus maripaludis
D-fructose 6-phosphate
40
-
pH 7.5, 30°C, phosphopfructokinase reaction
Methanococcus maripaludis
D-fructose
40
-
pH 6.5, 30°C
Methanococcus maripaludis
D-glucose
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
D-glucosamine
10 mM, 40% activation of glucokinase activity
Methanococcus maripaludis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Methanococcus maripaludis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
molecular modeling of structure. for binding of ADP, residues M347, I431 and L441 create a hydrophobic pocket around the adenine group. R194 makes a hydrogen bond with alpha and beta phosphates, carbonyl and NH groups from V432 peptide bond make a hydrogen bond with the NH2 group of C6 and the N1 atom of adenine
Methanococcus maripaludis
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.08
-
pH 7.5, 30°C, reverse glucokinase reaction
Methanococcus maripaludis
ADP
0.22
-
pH 6.5, 30°C; pH 7.5, 30°C, glucokinase reaction
Methanococcus maripaludis
D-fructose 6-phosphate
40
-
pH 7.5, 30°C, phosphopfructokinase reaction
Methanococcus maripaludis
D-fructose
40
-
pH 6.5, 30°C
Methanococcus maripaludis
D-glucose
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ADP
; strong inhibition effect in the reverse glucokinase reaction
Methanococcus maripaludis
AMP
strong substrate inhibition effect in the reverse glucokinase reaction
Methanococcus maripaludis
D-fructose
-
Methanococcus maripaludis
D-fructose 6-phosphate
; strong inhibition of glucokinase activity, competitive inhibion versus D-glucose as variable substrate
Methanococcus maripaludis
D-glucose
; substrate inhibition above 200 mM. At 10 mM 20% inhibition of phosphofructokinase activity
Methanococcus maripaludis
EDTA
50 mM, complete inhibition; complete loss of activity; completely abolishes activity
Methanococcus maripaludis
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.226
-
D-fructose 6-phosphate
pH 7.5, 30°C, glucokinase reaction
Methanococcus maripaludis
0.4
-
AMP
pH 7.5, 30°C, reverse glucokinase reaction
Methanococcus maripaludis
54
-
ADP
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
895
-
D-glucose
pH 7.5, 30°C
Methanococcus maripaludis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.065
-
D-fructose 6-phosphate
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
0.1
2
D-fructose 1,6-bisphosphate
pH 6.5, 30°C
Methanococcus maripaludis
0.1
2
D-glucose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
0.12
-
D-fructose 1,6-bisphosphate
pH 7.0, 30°C
Methanococcus maripaludis
8
-
ADP
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
40
-
D-glucose
pH 6.5, 30°C
Methanococcus maripaludis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
2 mM, about 70% of the activity with Mg2+; 2 mM, divalent metal ion required, activation of phosphofructokinase activity with Co2+ is about 70% compared to the activation with Mg2+, activation of glucokinase activity is about 35% compared to the activation with Mg2+; among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured
Methanococcus maripaludis
Mg2+
2 mM, divalent metal ion required, highest activity is observed in the presence of Mg2+; among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured; highest activity in the presence of Mg2+
Methanococcus maripaludis
Mn2+
2 mM, about 25% of the activity with Mg2+; 2 mM, divalent metal ion required, activation of phosphofructokinase activity with Co2+ is about 25% compared to the activation with Mg2+, activation of glucokinase activity is about 20% compared to the activation with Mg2+; among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured
Methanococcus maripaludis
additional information
divalent cation required, with highest activity in the presence of Mg2+
Methanococcus maripaludis
Ni2+
2 mM, divalent metal ion required, activation of phosphofructokinase activity with Co2+ is about 30% compared to the activation with Mg2+, activation of glucokinase activity is less than 10% compared to the activation with Mg2+; among the divalent metal cations tested, the highest activity is observed in the presence of Mg2+, although, in the presence of Co2+, Ni2+ and Mn2+, significant activity is also measured
Methanococcus maripaludis
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
Methanococcus maripaludis
-
AMP + D-fructose 1,6-bisphosphate
-
-
ir
ADP + D-glucose
Methanococcus maripaludis
the enzyme phosphorylates both D-glucose and D-fructose 6-phosphate. Binding of both substrates to the same active site. At a sugar concentration of 10 mM the acctivity with D-fructose 6-phosphate is about 75% compared to the activity with D-glucose. No activity in presence of ATP. kcat/KM for the phosphorylation of D-fructose 6-phosphate is 440fold higher than the kcat/Km for the phosphorylation of glucose. Analysis of the kcat/Km ratios shows that the glucose dephosphorylation is 2fold more effective than the phosphorylation
AMP + D-glucose 6-phosphate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
-
Methanococcus maripaludis
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
-
727486
Methanococcus maripaludis
AMP + D-fructose 1,6-bisphosphate
-
-
-
ir
ADP + D-fructose 6-phosphate
the bifunctional enzyme is able to phosphorylate D-glucose and beta-D-fructose 6-phosphate. The results of molecular modeling show that both sugars are bound to the enzyme by essentially the same residues except for N203, which establishes an interaction only when the substrate is D-fructose 6-phosphate, and E79, which interacts only with glucose. The enzyme shows higher activity with glucose compared to that obtained with beta-D-fructose 6-phosphate. beta-D-Fructose 6-phosphate shows 75% of the activity measured with glucose. In the presence of ATP, no activity is detected. Phosphatase activity is 67-fold lower than the kinase activity
727486
Methanococcus maripaludis
AMP + D-fructose 1,6-bisphosphate
-
-
-
ir
ADP + D-fructose 6-phosphate
the enzyme phosphorylates both D-glucose and D-fructose 6-phosphate. Binding of both substrates to the same active site. At a sugar concentration of 10 mM the activity with D-fructose 6-phosphate is about 75% compared to the activity with D-glucose. No activity in presence of ATP. kcat/KM for the phosphorylation of D-fructose 6-phosphate is 440fold higher than the kcat/Km for the phosphorylation of glucose
727486
Methanococcus maripaludis
AMP + D-fructose 1,6-bisphosphate
-
-
-
ir
ADP + D-fructose 6-phosphate
kinetics show hyperbolic behavior
727486
Methanococcus maripaludis
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
ADP + D-glucose
the enzyme phosphorylates both D-glucose and D-fructose 6-phosphate. Binding of both substrates to the same active site. At a sugar concentration of 10 mM the acctivity with D-fructose 6-phosphate is about 75% compared to the activity with D-glucose. No activity in presence of ATP. kcat/KM for the phosphorylation of D-fructose 6-phosphate is 440fold higher than the kcat/Km for the phosphorylation of glucose. Analysis of the kcat/Km ratios shows that the glucose dephosphorylation is 2fold more effective than the phosphorylation
727486
Methanococcus maripaludis
AMP + D-glucose 6-phosphate
-
-
-
r
ADP + D-glucose
the enzyme phosphorylates both D-glucose and D-fructose 6-phosphate.Binding of both substrates to the same active site. At a sugar concentration of 10 mM the acctivity with D-fructose 6-phosphate is about 75% compared to the activity with D-glucose. No activity in presence of ATP. kcat/KM for the phosphorylation of D-fructose 6-phosphate is 440fold higher than the kcat/Km for the phosphorylation of glucose. Analysis of the kcat/Km ratios shows that the glucose dephosphorylation is 2fold more effective than the phosphorylation
727486
Methanococcus maripaludis
AMP + D-glucose 6-phosphate
-
-
-
r
AMP + D-fructose 1,6-bisphosphate
-
727486
Methanococcus maripaludis
ADP + D-fructose 6-phosphate
-
-
-
r
CDP + beta-D-fructose 6-phosphate
about 15% compared to the activity with ADP
727486
Methanococcus maripaludis
CMP + D-fructose 1,6-bisphosphate
-
-
-
ir
additional information
less than 10% activity compared to the activity with D-glucose and ADP: L-rhamnose, D-arabinose, D-lyxose, D-fucose, D-galactose, D-mannose, D-fructose, 2-deoxyglucose, D-glucosamine, D-xylose, maltose, lactose
727486
Methanococcus maripaludis
?
-
-
-
-
additional information
bifunctional ADP-dependent phosphofructokinase/glucokinase, reactions of EC 2.7.1.147 and EC 2.7.1.146, respectively. The rate at which fructose 6-phosphate is phosphorylated is 440fold higher than the glucose phosphorylation rate
727486
Methanococcus maripaludis
?
-
-
-
-
UDP + D-glucose
the enzyme phosphorylates both D-glucose and D-fructose 6-phosphate. Activity with UDP and D-glucose is about 20% compared to the activity with ADP and D-glucose
727486
Methanococcus maripaludis
UMP + D-glucose 6-phosphate
-
-
-
r
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.45
-
D-fructose 1,6-bisphosphate
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
0.45
-
D-glucose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
16.5
-
D-fructose 6-phosphate
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
23
-
D-glucose
pH 6.5, 30°C
Methanococcus maripaludis
30
-
ADP
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
; phosphofructokinase activity
Methanococcus maripaludis
7
-
; glucokinase activity
Methanococcus maripaludis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
7
pH 5.0: about 50% of maximal activity, pH 7.0: about 65% of maximal activity; pH 5.0: about 50% of maximal phosphofructokinase activity, pH 7.0: about 65% of maximal phosphofructokinase activity
Methanococcus maripaludis
5.5
7.5
pH 5.5: about 50% of maximal phosphofructokinase activity, pH 7.5: about 75% of maximal phosphofructokinase activity
Methanococcus maripaludis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.57
-
D-glucose
pH 6.5, 30°C
Methanococcus maripaludis
1.09
-
D-glucose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
3
-
ADP
pH 6.5, 30°C
Methanococcus maripaludis
3.75
-
ADP
pH 7.0, 30°C
Methanococcus maripaludis
3.75
-
D-fructose 1,6-bisphosphate
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
253
-
D-fructose 6-phosphate
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.57
-
D-glucose
pH 6.5, 30°C
Methanococcus maripaludis
1.09
-
D-glucose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
3
-
ADP
pH 6.5, 30°C
Methanococcus maripaludis
3.75
-
ADP
pH 7.0, 30°C
Methanococcus maripaludis
3.75
-
D-fructose 1,6-bisphosphate
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
253
-
D-fructose 6-phosphate
pH 6.5, 30°C; pH 7.0, 30°C
Methanococcus maripaludis
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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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
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-