BRENDA - Enzyme Database
show all sequences of 2.7.1.147

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; substrate inhibition effect (Ki of 0.4 mM at 10 mM of glucose 6-phosphate). At a glucose 6-phosphate concentration of 0.5 mM, a sigmoidal behavior is observed, along with an even more pronounced inhibition
Methanococcus maripaludis
D-fructose
-
Methanococcus maripaludis
D-fructose 6-phosphate
competitive inhibition of D-fructose 6-phosphate when glucose is used as the variable substrate; 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
Methanococcus maripaludis
0.1
2
D-glucose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
0.62
-
D-glucose 6-phosphate
pH 7.0, 30°C
Methanococcus maripaludis
0.623
-
D-glucose 6-phosphate
pH 7.8, 30°C
Methanococcus maripaludis
16
-
ADP
pH 7.0, 30°C; pH 7.8, 30°C
Methanococcus maripaludis
40
-
D-glucose
pH 6.5, 30°C; pH 7.0, 30°C; pH 7.8, 30°C
Methanococcus maripaludis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
2 mM, about 40% 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 20% 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-glucose
Methanococcus maripaludis
-
AMP + D-glucose 6-phosphate
-
-
r
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
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-glucose
-
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
ADP + D-glucose
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
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-glucose 6-phosphate
-
727486
Methanococcus maripaludis
ADP + D-glucose
-
-
-
r
GDP + D-glucose
about 10% compared to the activity with ADP
727486
Methanococcus maripaludis
GMP + D-glucose 6-phosphate
-
-
-
r
additional information
less than 10% 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
?
-
-
-
-
TDP + D-glucose
about 10% compared to the activity with ADP
727486
Methanococcus maripaludis
TMP + D-glucose 6-phosphate
-
-
-
r
UDP + D-glucose
about 20% compared to the activity with ADP
727486
Methanococcus maripaludis
UMP + D-glucose 6-phosphate
-
-
-
r
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
UDP + D-glucose
about 20% of the activity with ADP
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-glucose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
0.678
-
D-glucose 6-phosphate
pH 7.8, 30°C
Methanococcus maripaludis
0.68
-
D-glucose 6-phosphate
pH 7.0, 30°C
Methanococcus maripaludis
16.5
-
D-fructose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
23
-
D-glucose
pH 6.5, 30°C; pH 7.0, 30°C; pH 7.8, 30°C
Methanococcus maripaludis
48
-
ADP
pH 7.0, 30°C; pH 7.8, 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 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
5.5
8
pH 5.5: about 50% of maximal activity, pH 8.0: about 30% of maximal 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; pH 7.8, 30°C
Methanococcus maripaludis
0.4
-
AMP
pH 7.5, 30°C, reverse glucokinase reaction; pH 7.8, 30°C. Substrate inhibition effect (Ki of 0.4 mM at 10 mM of glucose 6-phosphate). At a glucose 6-phosphate concentration of 0.5 mM, a sigmoidal behavior is observed, along with an even more pronounced inhibition
Methanococcus maripaludis
2
5
ADP
pH 7.0, 30°C; pH 7.8, 30°C, glucokinase
Methanococcus maripaludis
895
-
D-glucose
pH 7.0, 30°C; 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 7.5, 30°C, glucokinase reaction
Methanococcus maripaludis
D-fructose 6-phosphate
40
-
pH 7.5, 30°Cphosphopfructokinase reaction
Methanococcus maripaludis
D-fructose
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 7.5, 30°C, glucokinase reaction
Methanococcus maripaludis
D-fructose 6-phosphate
40
-
pH 7.5, 30°Cphosphopfructokinase reaction
Methanococcus maripaludis
D-fructose
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; substrate inhibition effect (Ki of 0.4 mM at 10 mM of glucose 6-phosphate). At a glucose 6-phosphate concentration of 0.5 mM, a sigmoidal behavior is observed, along with an even more pronounced inhibition
Methanococcus maripaludis
D-fructose
-
Methanococcus maripaludis
D-fructose 6-phosphate
competitive inhibition of D-fructose 6-phosphate when glucose is used as the variable substrate; 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; pH 7.8, 30°C
Methanococcus maripaludis
0.4
-
AMP
pH 7.5, 30°C, reverse glucokinase reaction; pH 7.8, 30°C. Substrate inhibition effect (Ki of 0.4 mM at 10 mM of glucose 6-phosphate). At a glucose 6-phosphate concentration of 0.5 mM, a sigmoidal behavior is observed, along with an even more pronounced inhibition
Methanococcus maripaludis
2
5
ADP
pH 7.0, 30°C; pH 7.8, 30°C, glucokinase
Methanococcus maripaludis
895
-
D-glucose
pH 7.0, 30°C; 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
Methanococcus maripaludis
0.1
2
D-glucose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
0.62
-
D-glucose 6-phosphate
pH 7.0, 30°C
Methanococcus maripaludis
0.623
-
D-glucose 6-phosphate
pH 7.8, 30°C
Methanococcus maripaludis
16
-
ADP
pH 7.0, 30°C; pH 7.8, 30°C
Methanococcus maripaludis
40
-
D-glucose
pH 6.5, 30°C; pH 7.0, 30°C; pH 7.8, 30°C
Methanococcus maripaludis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
2 mM, about 40% 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 20% 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-glucose
Methanococcus maripaludis
-
AMP + D-glucose 6-phosphate
-
-
r
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
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-glucose
-
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
ADP + D-glucose
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
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-glucose 6-phosphate
-
727486
Methanococcus maripaludis
ADP + D-glucose
-
-
-
r
GDP + D-glucose
about 10% compared to the activity with ADP
727486
Methanococcus maripaludis
GMP + D-glucose 6-phosphate
-
-
-
r
additional information
less than 10% 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
?
-
-
-
-
TDP + D-glucose
about 10% compared to the activity with ADP
727486
Methanococcus maripaludis
TMP + D-glucose 6-phosphate
-
-
-
r
UDP + D-glucose
about 20% compared to the activity with ADP
727486
Methanococcus maripaludis
UMP + D-glucose 6-phosphate
-
-
-
r
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
UDP + D-glucose
about 20% of the activity with ADP
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-glucose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
0.678
-
D-glucose 6-phosphate
pH 7.8, 30°C
Methanococcus maripaludis
0.68
-
D-glucose 6-phosphate
pH 7.0, 30°C
Methanococcus maripaludis
16.5
-
D-fructose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
23
-
D-glucose
pH 6.5, 30°C; pH 7.0, 30°C; pH 7.8, 30°C
Methanococcus maripaludis
48
-
ADP
pH 7.0, 30°C; pH 7.8, 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 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
5.5
8
pH 5.5: about 50% of maximal activity, pH 8.0: about 30% of maximal 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
0.575
-
D-glucose
pH 7.8, 30°C
Methanococcus maripaludis
0.58
-
D-glucose
pH 7.0, 30°C
Methanococcus maripaludis
1.09
-
D-glucose 6-phosphate
pH 6.5, 30°C; pH 7.8, 30°C
Methanococcus maripaludis
1.1
-
D-glucose 6-phosphate
pH 7.0, 30°C
Methanococcus maripaludis
3
-
ADP
pH 7.0, 30°C; pH 7.8, 30°C
Methanococcus maripaludis
253
-
D-fructose 6-phosphate
pH 6.5, 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
0.575
-
D-glucose
pH 7.8, 30°C
Methanococcus maripaludis
0.58
-
D-glucose
pH 7.0, 30°C
Methanococcus maripaludis
1.09
-
D-glucose 6-phosphate
pH 6.5, 30°C; pH 7.8, 30°C
Methanococcus maripaludis
1.1
-
D-glucose 6-phosphate
pH 7.0, 30°C
Methanococcus maripaludis
3
-
ADP
pH 7.0, 30°C; pH 7.8, 30°C
Methanococcus maripaludis
253
-
D-fructose 6-phosphate
pH 6.5, 30°C
Methanococcus maripaludis
Other publictions for EC 2.7.1.147
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)
738699
Richter
The Structural and functional ...
Homo sapiens
J. Biol. Chem.
291
3694-3704
2016
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1
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738242
Abarca-Lagunas
Dissecting the functional role ...
Thermococcus litoralis, Thermococcus litoralis DSM 5473
FEBS Lett.
589
3271-3276
2015
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4
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5
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10
10
727486
Castro-Fernandez
Bifunctional ADP-dependent pho ...
Methanococcus maripaludis
FEBS J.
281
2017-2029
2014
1
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1
1
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6
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13
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6
2
3
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7
7
728613
Rivas-Pardo
Crystal structure, SAXS and ki ...
Thermococcus litoralis, Thermococcus litoralis DSM 5473
PLoS One
8
e66687
2013
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1
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6
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737805
Qian
Thermal stability of glucokina ...
Caldanaerobacter subterraneus subsp. tengcongensis, Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242
BioMed Res. Int.
2013
646539
2013
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2
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2
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2
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6
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1
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739468
Richter
Zinc finger nuclease mediated ...
Homo sapiens
PLoS ONE
8
e65267
2013
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1
1
-
-
-
721764
Merino
Catalytic and regulatory roles ...
Pyrococcus furiosus, Pyrococcus horikoshii, Thermococcus litoralis
Biochimie
94
516-524
2012
-
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3
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3
8
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12
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3
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3
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9
3
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3
3
8
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12
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3
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3
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-
9
3
-
-
-
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-
-
9
9
721992
Kaminski
T cell activation is driven by ...
Homo sapiens
Cell Rep.
2
1300-1315
2012
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2
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2
1
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1
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-
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1
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-
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-
2
2
-
-
-
723169
Richter
Expression and role in glycoly ...
Homo sapiens
Mol. Cell. Biochem.
364
131-145
2012
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1
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5
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19
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19
-
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1
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1
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1
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-
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2
2
-
-
-
660867
Ronimus
Cloning and biochemical charac ...
Mus musculus
Biochem. Biophys. Res. Commun.
315
652-658
2004
1
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1
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4
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7
1
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2
1
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-
660831
Labes
ADP-dependent glucokinase from ...
Archaeoglobus fulgidus, Archaeoglobus fulgidus 7324
Arch. Microbiol.
180
69-75
2003
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8
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1
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662610
Ito
Crystal structure of an ADP-de ...
Pyrococcus furiosus
J. Mol. Biol.
331
871-883
2003
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1
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6
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1
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5
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1
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1
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1
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1
1
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1
1
1
6
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1
1
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1
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1
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1
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2
1
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-
-
-
395244
Sakuraba
ADP-dependent glucokinase/phos ...
Methanocaldococcus jannaschii
J. Biol. Chem.
277
12495-12498
2002
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1
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6
2
1
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1
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1
1
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1
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6
2
1
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1
1
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-
-
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395245
Verhees
Biochemical adaptations of two ...
Pyrococcus furiosus
Biochem. J.
366
121-127
2002
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1
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4
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663324
Tsuge
Crystal structure of the ADP-d ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Protein Sci.
11
2456-2463
2002
-
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1
1
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1
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2
-
48
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1
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4
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1
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1
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1
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1
1
1
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1
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4
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1
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395241
Ito
Structural basis for the ADP-s ...
Thermococcus litoralis
Structure
9
205-214
2001
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1
1
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395242
Kengen
ADP-dependent glucokinase and ...
Pyrococcus furiosus
Methods Enzymol.
331
41-53
2001
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1
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3
2
1
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1
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1
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2
1
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1
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1
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1
1
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1
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-
-
-
-
-
-
-
-
721449
Labes
Sugar utilization in the hyper ...
Archaeoglobus fulgidus, Archaeoglobus fulgidus 7324
Arch. Microbiol.
176
329-338
2001
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-
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2
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1
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9
-
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2
2
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2
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1
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-
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-
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2
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1
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2
2
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2
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1
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-
1
1
-
-
-
746520
Ito
Structural basis for the ADP- ...
Thermococcus litoralis, Thermococcus litoralis DSM 5473
Structure
9
205-214
2001
-
-
1
1
-
-
-
-
-
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8
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1
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-
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1
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1
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1
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1
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1
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-
395243
Koga
Biochemical characterization, ...
Pyrococcus furiosus, Thermococcus litoralis
J. Biochem.
128
1079-1085
2000
-
-
-
-
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4
4
2
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2
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2
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1
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4
2
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2
-
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4
4
2
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2
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1
-
4
2
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2
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-
-
-
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-
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-
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395240
Kengen
Purification and characterizat ...
Pyrococcus furiosus
J. Biol. Chem.
270
30453-30457
1995
-
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2
1
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3
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1
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1
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1
1
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1
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1
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1
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1
-
1
1
-
-
1
-
-
-
-
-
-
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-
-
-
-
722596
Kengen
Evidence for the operation of ...
Pyrococcus furiosus
J. Biol. Chem.
269
17537-17541
1994
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