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ADP + D-fructose
AMP + D-fructose 6-phosphate
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
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
-
-
ir
ADP + D-glucosamine
AMP + D-glucosamine 6-phosphate
ADP + D-glucose
AMP + D-glucose 6-phosphate
ADP + D-mannose
AMP + D-mannose 6-phosphate
ADP + N-acetyl-D-glucosamine
AMP + N-acetyl-D-glucosamine 6-phosphate
the enzyme exhibits a low level of activity against N-acetyl-D-glucosamine
-
-
?
AMP + D-glucose 6-phosphate
ADP + D-glucose
-
-
-
r
CDP + D-glucose
CMP + D-glucose 6-phosphate
12% of the activity with ADP
-
-
?
D-1,5-anhydroglucitol + ADP
?
D-glucose + ADP
D-glucose 6-phosphate + AMP
GDP + D-glucose
GMP + D-glucose 6-phosphate
TDP + D-glucose
TMP + D-glucose 6-phosphate
about 10% compared to the activity with ADP
-
-
r
UDP + D-glucose
UMP + D-glucose 6-phosphate
additional information
?
-
ADP + D-fructose
AMP + D-fructose 6-phosphate
10% of the activity with D-glucose
-
-
?
ADP + D-fructose
AMP + D-fructose 6-phosphate
-
ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant
-
-
?
ADP + D-glucosamine
AMP + D-glucosamine 6-phosphate
-
the enzyme is highly specific for both substrates
-
-
r
ADP + D-glucosamine
AMP + D-glucosamine 6-phosphate
-
the enzyme is highly specific for both substrates
-
-
r
ADP + D-glucosamine
AMP + D-glucosamine 6-phosphate
-
-
-
?
ADP + D-glucosamine
AMP + D-glucosamine 6-phosphate
the enzyme functions as the glucosamine kinase responsible for the chitin degradation
-
-
?
ADP + D-glucosamine
AMP + D-glucosamine 6-phosphate
-
-
-
?
ADP + D-glucosamine
AMP + D-glucosamine 6-phosphate
the enzyme functions as the glucosamine kinase responsible for the chitin degradation
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
first step of the Embden-Meyerhoff pathway
-
-
r
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
the enzyme is highly specific for both substrates
-
-
r
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
diphosphate and ATP do not serve as phosphoryl donor
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
first step of the Embden-Meyerhoff pathway
-
-
r
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
the enzyme is highly specific for both substrates
-
-
r
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
enzyme shows substrate inhibition at high glucose concentrations
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
r
ADP + D-glucose
AMP + D-glucose 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 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
-
-
r
ADP + D-glucose
AMP + D-glucose 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
-
-
r
ADP + D-glucose
AMP + D-glucose 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 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
-
-
r
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
best substrate concentration is 0.35 mM glucose, high concentrations are inhibitory
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
step of the Embden-Meyerhoff pathway
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
substrate binding site structure, glucose-induced conformational change and domain closure in the enzyme
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
catalysis follows a sequential ordered mechanism
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
catalysis follows a sequential ordered mechanism
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
-
-
-
-
?
ADP + D-mannose
AMP + D-mannose 6-phosphate
17% of the velocity with D-glucose
-
-
?
ADP + D-mannose
AMP + D-mannose 6-phosphate
17% of the velocity with D-glucose
-
-
?
ADP + D-mannose
AMP + D-mannose 6-phosphate
20% of the activity with D-glucose
-
-
?
D-1,5-anhydroglucitol + ADP
?
-
-
-
-
?
D-1,5-anhydroglucitol + ADP
?
-
-
-
-
?
D-glucose + ADP
D-glucose 6-phosphate + AMP
-
ADP can be replaced by GDP and CDP to a limited extent
-
-
?
D-glucose + ADP
D-glucose 6-phosphate + AMP
-
-
-
-
?
D-glucose + ADP
D-glucose 6-phosphate + AMP
-
-
-
?
D-glucose + ADP
D-glucose 6-phosphate + AMP
-
CDP shows comparable activity
-
-
ir
D-glucose + ADP
D-glucose 6-phosphate + AMP
-
-
-
?
D-glucose + ADP
D-glucose 6-phosphate + AMP
-
CDP shows comparable activity
-
-
ir
GDP + D-glucose
GMP + D-glucose 6-phosphate
-
-
-
?
GDP + D-glucose
GMP + D-glucose 6-phosphate
about 10% compared to the activity with ADP
-
-
r
GDP + D-glucose
GMP + D-glucose 6-phosphate
55% of the activity with ADP
-
-
?
UDP + D-glucose
UMP + D-glucose 6-phosphate
about 20% compared to the activity with ADP
-
-
r
UDP + D-glucose
UMP + D-glucose 6-phosphate
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
-
-
r
UDP + D-glucose
UMP + D-glucose 6-phosphate
about 20% of the activity with ADP
-
-
r
additional information
?
-
-
2-deoxyglucose is a poor substrate, no activity with ATP, CDP, UDP, or GDP as phosphate donors, no activity with mannose, fructose, and fructose 6-phosphate as phosphate acceptors
-
-
?
additional information
?
-
-
2-deoxyglucose is a poor substrate, no activity with ATP, CDP, UDP, or GDP as phosphate donors, no activity with mannose, fructose, and fructose 6-phosphate as phosphate acceptors
-
-
?
additional information
?
-
enzyme effectively utilizes glucose and cannot efficiently catalyze mannose, and 2-deoxyglucose. No activity with ATP, CTP, GTP, phosphoenolpyruvate
-
-
?
additional information
?
-
enzyme effectively utilizes glucose and cannot efficiently catalyze mannose, and 2-deoxyglucose. No activity with ATP, CTP, GTP, phosphoenolpyruvate
-
-
?
additional information
?
-
poor activity with CDP. No substrates: ATP, 2-deoxyglucose, L-glucose, methyl-beta-D-xylopyranoside, D-glucosamine, L-rhamnose, D-tagatose, 3-O-methyl-D-glucopyranoside, 1-O-methyl-beta-D-glucopyranoside, 1-O-methyl-alpha-D-glucopyranoside, D-arabinose, L-arabinose, myo-inositol, D-ribose, D-xylose, D-galactose, D-fructose, D-mannose, D-fructose-6-phosphate, and alpha-D-glucose-1-phosphate
-
-
?
additional information
?
-
the enzyme from Methanococcus jannaschii also shows phosphofructokinase activity, a bifunctional MjPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanococcus jannaschii also shows phosphofructokinase activity, a bifunctional MjPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanococcoides burtonii also shows glucokinase activity, a bifunctional PFK/GK enzyme. Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminus, where the catalytic GXGD motif is located, but it is able to show glucokinase activity. Substrate specificity analysis, structure-function analysis
-
-
-
additional information
?
-
-
the enzyme from Methanococcoides burtonii also shows glucokinase activity, a bifunctional PFK/GK enzyme. Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminus, where the catalytic GXGD motif is located, but it is able to show glucokinase activity. Substrate specificity analysis, structure-function analysis
-
-
-
additional information
?
-
the enzyme from Methanococcoides burtonii also shows glucokinase activity, a bifunctional PFK/GK enzyme. Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminus, where the catalytic GXGD motif is located, but it is able to show glucokinase activity. Substrate specificity analysis, structure-function analysis
-
-
-
additional information
?
-
the enzyme from Methanococcoides burtonii also shows glucokinase activity, a bifunctional PFK/GK enzyme. Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminus, where the catalytic GXGD motif is located, but it is able to show glucokinase activity. Substrate specificity analysis, structure-function analysis
-
-
-
additional information
?
-
the enzyme from Methanococcoides burtonii also shows glucokinase activity, a bifunctional PFK/GK enzyme. Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminus, where the catalytic GXGD motif is located, but it is able to show glucokinase activity. Substrate specificity analysis, structure-function analysis
-
-
-
additional information
?
-
the enzyme from Methanococcoides burtonii also shows glucokinase activity, a bifunctional PFK/GK enzyme. Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminus, where the catalytic GXGD motif is located, but it is able to show glucokinase activity. Substrate specificity analysis, structure-function analysis
-
-
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
no activity with ATP, GTP, CTP, UTP, TTP, diphosphate, polyphosphate, TDP, UDP, acetyl-phosphate, phosphoarginine, carbamoyl phosphate, phosphocreatine, and phosphoenolpyruvate as phosphoryl donors
-
-
?
additional information
?
-
-
no activity with ATP, GTP, CTP, UTP, TTP, diphosphate, polyphosphate, TDP, UDP, acetyl-phosphate, phosphoarginine, carbamoyl phosphate, phosphocreatine, and phosphoenolpyruvate as phosphoryl donors
-
-
?
additional information
?
-
-
substrate-induced fit, binding of ADP induces large conformational changes
-
-
?
additional information
?
-
-
substrate-induced fit, binding of ADP induces large conformational changes
-
-
?
additional information
?
-
-
activity is not observed toward chitobiose and N-,N-diacetylchitobiose
-
-
-
additional information
?
-
activity is not observed toward chitobiose and N-,N-diacetylchitobiose
-
-
-
additional information
?
-
catalysis follows a sequential ordered mechanism
-
-
?
additional information
?
-
-
catalysis follows a sequential ordered mechanism
-
-
?
additional information
?
-
the glucokinase from Thermococcus litoralis shows no activity with fructose 6-phosphate
-
-
-
additional information
?
-
the glucokinase from Thermococcus litoralis shows no activity with fructose 6-phosphate
-
-
-
additional information
?
-
catalysis follows a sequential ordered mechanism
-
-
?
additional information
?
-
-
the enzyme also shows phosphofructokinase activity, a bifunctional AncMsPFK/GK ancestor enzyme
-
-
-
additional information
?
-
-
the enzyme also shows phosphofructokinase activity, a bifunctional AncPFK/GK ancestor enzyme
-
-
-
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Ca2+
-
-
Co2+
-
-
Co2+
activates to less than 50% activity compared to Mg2+ activation
Co2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
Co2+
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+
Co2+
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
Co2+
2 mM, about 40% of the activity with Mg2+
Co2+
activates to less than 50% activity compared to Mg2+ activation
Co2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
Co2+
-
highest kcat/Km value obtained
KCl
activates at up to 0.5 M, inhibitory above about 1.0 M
KCl
required at 0.5 M for full enzyme activity
KCl
-
has no evident effect on the AncMsPFK/GK activity
Mg2+
-
at 4 mM, optimal ratio of ADP:MgCl2 is 1:2
Mg2+
-
required for activation
Mg2+
required, activates, preferred divalent cation
Mg2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
Mg2+
highest activity in the presence of Mg2+
Mg2+
2 mM, divalent metal ion required, highest activity is observed in the presence of Mg2+
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
Mg2+
required, activates, preferred divalent cation
Mg2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
Mg2+
best at ADP-Mg2+ ratio of 1:1, excess Mg2+ is inhibitory
Mg2+
-
required for activation
Mg2+
binding site structure
Mg2+
-
highest kcat/Km value obtained
Mg2+
-
highest kcat/Km value obtained
Mg2+
-
required for activation
Mn2+
-
-
Mn2+
activates to less than 50% activity compared to Mg2+ activation
Mn2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
Mn2+
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+
Mn2+
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
Mn2+
2 mM, about 20% of the activity with Mg2+
Mn2+
activates to less than 50% activity compared to Mg2+ activation
Mn2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
Mn2+
-
highest kcat/Km value obtained
Ni2+
-
-
Ni2+
activates to less than 50% activity compared to Mg2+ activation
Ni2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
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+
Ni2+
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
Ni2+
activates to less than 50% activity compared to Mg2+ activation
Ni2+
the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+
additional information
-
divalent cations are required, Mg2+, Mn2+, and Ca2+ are most effective, Cu2+, Zn2+, Ni2+, and Cu2+ can partially substitute
additional information
Ca2+ or Cu2+ cannot substitute for Mg2+
additional information
poor activation by Ca2+ probably due to steric hindrance
additional information
-
poor activation by Ca2+ probably due to steric hindrance
additional information
divalent cation required, with highest activity in the presence of Mg2+
additional information
-
divalent cation required, with highest activity in the presence of Mg2+
additional information
poor activation by Ca2+ probably due to steric hindrance
additional information
-
poor activation by Ca2+ probably due to steric hindrance
additional information
-
ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant
additional information
-
ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant
additional information
-
ADP-dependent kinase is regulated by divalent metal cations due to binding of this ligand to a second site. Results show that a complex between a divalent metal cation and the nucleotide is required for the phosphoryl transfer reaction. The presence of a second metal binding site is suggested which regulates the activity by producing an enzyme with a reduced catalytic constant
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evolution
-
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
evolution
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
evolution
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
evolution
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
evolution
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons
evolution
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
evolution
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
-
evolution
-
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
consensus phylogenetic tree of the ADP-dependent sugar kinases family, evolutionary history of enzyme substrate affinity, reconstruction
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanohalobium evestigatum posseses a bifunctional MevePFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
evolution
-
the enzyme belongs to the ADP-dependent phosphofructokinase/glucokinase family. Homology modeling of ADP-dependent sugar kinases from Halobacteria, Methanosarcinales and Eukarya, overview. Models built are divided into four groups based on the taxonomic categorization of the source organism and their ability to grow in high salinity environments as reported in the literature. The groups defined are: Halobacteria, halophilic Methanosarcinales, non-halophilic Methanosarcinales, and Eukarya, the latter used as a control outgroup. Sequences and structures comparisons. Methanosarcina mazei posseses a bifunctional MmazPFK/GK
-
evolution
-
kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
malfunction
-
down-regulation of ADPGK or GPD2 abundance inhibits oxidative signal generation and induction of NF-kappaB-dependent gene expression, whereas over-expression of ADPGK potentiates them
malfunction
-
overexpression or suppression of ADPGK does not show any relevant effect
malfunction
ADPGK knock-out Ramos BL cells display abated in vitro and in vivo tumour aggressiveness, via tumour-macrophage co-culture, migration and Zebrafish xenograft studies. Perturbed glycolysis and visibly reduced markers of Warburg effect in ADPGK knock-out cells, finally leading to apoptosis. Knock-out cells show repression of MYC proto-oncogene, and up to four-fold reduction in accumulated mutations in translocated MYC
malfunction
-
ADPGK knockdown in zebrafish embryos leads to short, dorsalized body axis induced by elevated apoptosis. ADPGK hypomorphic zebrafish display dysfunctional glucose metabolism
malfunction
TK1110 disruption results in almost complete impairment in chitin degradation, and a complete loss of chitin-dependent H2 production
malfunction
upon activation, ADPGK knockout Jurkat T cells display increased cell death and ER stress. The increase in cell death results from a metabolic catastrophe and knockout cells displayed severely disturbed energy metabolism hindering induction of Warburg phenotype
malfunction
-
TK1110 disruption results in almost complete impairment in chitin degradation, and a complete loss of chitin-dependent H2 production
-
metabolism
-
human ADPGK catalyses ADP-dependent phosphorylation of glucose in vitro
metabolism
enzyme TK1110 functions as the glucosamine kinase responsible for the chitin degradation in Thermococcus kodakarensis
physiological function
-
T cell activation-induced mitochondrial ROS production and NF-kappaB-driven gene expression depend on activation of ADPGK. ADPGK activation is accompanied by a rapid glucose uptake, downregulation of mitochondrial oxygen consumption, and deviation of glycolysis toward the glycerol-3-phosphate dehydrogenase shuttle
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
-
knockout of inc finger nucleases in each H-460 and HCT-11 cells lead to frameshift mutations in all alleles at the target site in exon 1 of ADP-dependent glucokinase ADPGK, and are ADPGK-null by immunoblotting. ADPGK knockout has little or noeffect on cell proliferation, but compromises the ability of H-460 cells to survive siRNA silencing of hexokinase-2 under oxic conditions and anoxia. No such changes are found when ADPGK is knocked out in HCT-116 cells. Knockout of ADPGK in HCT-116 cells causes few changes in global gene expression, while knockout of ADPGK in H-460 cells causes notable up-regulation of mRNAs encoding cell adhesion proteins. No consistent effect on glycolysis under oxic conditions in a variety of media is observed. Oxygen consumption rates are generally lower in the ADPGK knockouts
physiological function
the enzyme functions as the glucosamine kinase responsible for the chitin degradation
physiological function
-
the enzyme plays a critical role in T cell receptor activation-induced remodeling of energy metabolism. The enzyme is part of a glucose sensing system in the ER modulating metabolism via regulation of N- and O-glycosylation
physiological function
the enzyme plays a critical role in T cell receptor activation-induced remodeling of energy metabolism. The enzyme is part of a glucose sensing system in the ER modulating metabolism via regulation of N- and O-glycosylation
physiological function
the enzyme plays a major role in T-cell activation and induction of Warburg effect
physiological function
-
the enzyme functions as the glucosamine kinase responsible for the chitin degradation
-
additional information
enzyme structure and homology modeling
additional information
-
enzyme structure and homology modeling
additional information
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
additional information
-
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
additional information
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
additional information
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
-
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
-
additional information
-
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
-
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
molecular modeling, docking with D-glucose and D-fructose 6-phosphate, and molecular dynamics
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling
-
additional information
-
enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211
-
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sitting drop vapor diffusion method at 20°C, complex of the enzyme with glucose and 8-bromoadenosine phosphate
structures reveal a ribokinase-like tertiary fold similar to archaeal orthologues but with significant differences in some secondary structural elements. Both the unliganded and the AMP-bound ADPGK structures are in the open conformation and reveal the presence of a disulfide bond between conserved cysteines that is positioned at the nucleotide-binding loop. The AMP-bound structure defines the nucleotide-binding site with one of the disulfide bond cysteines coordinating the AMP with its main chain atoms
sitting drop vapor diffusion method at 20°C, crystal structure of the ADP-dependent glucokinase from Methanocaldococcus jannaschii in complex with the inhibitor 5-iodotubercidin
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
purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein, 2.5 mM ADP, 200 mM NaCl, 7.5 mM MgCl2, 25 mM HEPES, pH 7.8, and 1 mM 2-mercaptoethanol with 0.001 ml of reservoir solution containing 20 mM CdCl2, 20 mM MgCl2, 20 mM NiCl2, 24% PEG MME 2000, and 100 mM sodium acetate, pH 4.5, 2 weeks, 19C, X-ray diffraction structure determination and analysis at 1.46 A resolution, molecular replacement using the structure of the ancestral ADP-dependent kinase (PDB ID 5K27) split into small and large domains as search models
enzyme in complex with AMP, sitting drop vapour diffusion method, 10 mg/ml protein in 6 mM ADP-beta-S, 30 mM glucose mixed in equal volumes with reservoir solution containing 1.6 M citrate, pH 6.5, 10 mM DTT, equilibration against 0.075 ml of reservoir solution at 25°C, a few weeks to 1 month, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement, modeling
purified recombinant N-terminally His-tagged apoenzyme, hanging drop vapour diffusion method, 20°C, 10 mg/ml protein in solution is mixed with an equal volume of 0.003 ml of mother liquor containing 9-13% PEG 6000, 0.2 M Li2SO4, and 0.1 M citrate buffer, pH 3.6, heavy atom derivatization with HgCl2, X-ray diffraction structure determination and analysis at 2.0 A resolution, single isomorphous replacement with an anomalous scattering
-
sitting drop vapor diffusion method at 20°C, complex of the enzyme with glucose and 8-bromoadenosine phosphate
2.3 A resolution, R-factor of 20.4%
crystal structures of apo form and holo form, in the presence of D-glucose and the nonhydrolyzable ADP analog adenosine 5'-(3-thio)diphosphate. The conformational changes upon sequential substrate binding can be explained by an almost pure rotation (or a rotation plus a translation) facilitated by residues in the flexible inter-domain connection
crystallized with ADP and Mg2+, the structure is determined by multiple isomorphous replacement with anomalous scattering and refined at 2.3 A. Crystals are grown at 25°C by the hanging drop vapor diffusion method
sitting-drop vapor-diffusion crystallization
purified enzyme mutant E72A, hanging drop vapor diffusion method, mixing of 0.002 ml of 8 mg/ml protein in 25 mM HEPES/NaOH, pH 7.8, 30 mM MgCl2, 20 mM fructose 6-phosphate, and 20 mM AMP with 0.002 ml of reservoir solution containing 18% PEG 3350 and 0.15 M NaI, 3 days at 18°C, X-ray diffraction structure determination and analysis at 2.61 A resolution, molecular replacement using the structure of Pyrococcus horikoshii ADP-PFK (PDB ID 3DRW) split into small and large domains as search models
-
purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein, 2.5 mM ADP, 200 mM NaCl, 7.5 mM MgCl2, 25 mM HEPES, pH 7.8, and 1 mM 2-mercaptoethanol with 0.001 ml of reservoir solution containing 20 mM CdCl2, 20 mM MgCl2, 20 mM NiCl2, 24% PEG MME 2000, and 100 mM sodium acetate, pH 4.5, 2 weeks, 19°C, X-ray diffraction structure determination and analysis at 2.86 A resolution, molecular replacement using the structure of the ancestral ADP-dependent kinase (PDB ID 5K27) split into small and large domains as search models
-
purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein, 2.5 mM ADP, 200 mM NaCl, 7.5 mM MgCl2, 25 mM HEPES, pH 7.8, and 1 mM 2-mercaptoethanol with 0.001 ml of reservoir solution containing 20 mM CdCl2, 20 mM MgCl2, 20 mM NiCl2, 24% PEG MME 2000, and 100 mM sodium acetate, pH 4.5, 2 weeks, 19C, X-ray diffraction structure determination and analysis at 1.46 A resolution, molecular replacement using the structure of the ancestral ADP-dependent kinase (PDB ID 5K27) split into small and large domains as search models
purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein, 2.5 mM ADP, 200 mM NaCl, 7.5 mM MgCl2, 25 mM HEPES, pH 7.8, and 1 mM 2-mercaptoethanol with 0.001 ml of reservoir solution containing 20 mM CdCl2, 20 mM MgCl2, 20 mM NiCl2, 24% PEG MME 2000, and 100 mM sodium acetate, pH 4.5, 2 weeks, 19C, X-ray diffraction structure determination and analysis at 1.46 A resolution, molecular replacement using the structure of the ancestral ADP-dependent kinase (PDB ID 5K27) split into small and large domains as search models
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