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acetyl-phosphate + D-fructose 6-phosphate
acetate + D-fructose 1,6-bisphosphate
ADP + 2'-deoxyadenosine
AMP + ?
-
-
-
?
ADP + 2'-deoxyadenosine
AMP + dAMP
-
-
-
r
ADP + adenosine
2 AMP
-
-
-
r
ADP + adenosine
AMP + ?
-
-
-
?
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
-
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
ADP + D-glucose
AMP + D-glucose 6-phosphate
ADP + ribose 5-phosphate
AMP + ?
-
-
-
?
ADP + ribose 5-phosphate
AMP + ribose 1,5-bisphosphate
-
-
-
r
ADP + thymidine
AMP + ?
-
-
-
?
ADP + thymidine
AMP + TMP
-
-
-
r
AMP + D-fructose 1,6-bisphosphate
ADP + D-fructose 6-phosphate
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
CDP + beta-D-fructose 6-phosphate
CMP + D-fructose 1,6-bisphosphate
about 15% compared to the activity with ADP
-
-
ir
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
D-fructose 6-phosphate + CDP
D-fructose 1,6-bisphosphate + CMP
D-fructose 6-phosphate + GDP
D-fructose 1,6-bisphosphate + GMP
D-fructose 6-phosphate + IDP
D-fructose 1,6-bisphosphate + IMP
D-fructose 6-phosphate + UDP
D-fructose 1,6-bisphosphate + UMP
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
additional information
?
-
acetyl-phosphate + D-fructose 6-phosphate
acetate + D-fructose 1,6-bisphosphate
activity is 83% compared to the activity with ADP
-
-
?
acetyl-phosphate + D-fructose 6-phosphate
acetate + D-fructose 1,6-bisphosphate
activity is 83% compared to the activity with ADP
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
enzyme is highly specific for D-fructose 6-phosphate in the forward reaction
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
diphosphate and ATP do not serve as phosphoryl donors
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
key enzyme of the glycolytic pathway
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
activity with GDP is 1.4% compared to the activity with ADP, activity with ATP is 0.3% compared to the activity with ADP, activity with GTP is 8.1% compared to the activity with ADP, no activity with diphosphate, phosphoenolpyruvate or polyphosphate
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
key enzyme of the glycolytic pathway
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
activity with GDP is 1.4% compared to the activity with ADP, activity with ATP is 0.3% compared to the activity with ADP, activity with GTP is 8.1% compared to the activity with ADP, no activity with diphosphate, phosphoenolpyruvate or polyphosphate
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
ir
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
the bifunctional enzyme is able to phosphorylate D-glucose and beta-D-fructose 6-phosphate. The results of molecular modeling show that both sugars are bound to the enzyme by essentially the same residues except for N203, which establishes an interaction only when the substrate is D-fructose 6-phosphate, and E79, which interacts only with glucose. The enzyme shows higher activity with glucose compared to that obtained with beta-D-fructose 6-phosphate. beta-D-Fructose 6-phosphate shows 75% of the activity measured with glucose. In the presence of ATP, no activity is detected. Phosphatase activity is 67-fold lower than the kinase activity
-
-
ir
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-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
kinetics show hyperbolic behavior
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
the rate of dephosphorylation of fructose 1,6-bisphosphate is 3times lower at 50°C than the phosphorylation of fructose 6-phosphate
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
-
?
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 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
cf. EC 2.7.1.147
-
-
r
AMP + D-fructose 1,6-bisphosphate
ADP + D-fructose 6-phosphate
-
-
-
r
AMP + D-fructose 1,6-bisphosphate
ADP + D-fructose 6-phosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
only 20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP. No significant activity is detected in the presence of other phosphoryl donors examined
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
only 20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP. No significant activity is detected in the presence of other phosphoryl donors examined
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
only 20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP. No significant activity is detected in the presence of other phosphoryl donors examined
-
-
r
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
-
ADP can be replaced by GDP and CDP to a limited extent
-
-
?
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
ADP can be replaced by acetylphosphate
-
-
?
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
ADP can be replaced by acetylphosphate
-
-
ir
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
-
ADP can be replaced by GDP, ATP and GTP to a limited extent
-
-
?
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
-
ADP can be replaced by GDP, ATP and GTP to a limited extent
-
-
ir
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
100% activity
-
-
?
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
100% activity
-
-
?
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
-
-
-
-
r
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
-
-
-
r
D-fructose 6-phosphate + CDP
D-fructose 1,6-bisphosphate + CMP
about 35% activity compared to ADP
-
-
?
D-fructose 6-phosphate + CDP
D-fructose 1,6-bisphosphate + CMP
about 35% activity compared to ADP
-
-
?
D-fructose 6-phosphate + GDP
D-fructose 1,6-bisphosphate + GMP
about 50% activity compared to ADP
-
-
?
D-fructose 6-phosphate + GDP
D-fructose 1,6-bisphosphate + GMP
about 50% activity compared to ADP
-
-
?
D-fructose 6-phosphate + IDP
D-fructose 1,6-bisphosphate + IMP
about 50% activity compared to ADP
-
-
?
D-fructose 6-phosphate + IDP
D-fructose 1,6-bisphosphate + IMP
about 50% activity compared to ADP
-
-
?
D-fructose 6-phosphate + UDP
D-fructose 1,6-bisphosphate + UMP
about 105% activity compared to ADP
-
-
?
D-fructose 6-phosphate + UDP
D-fructose 1,6-bisphosphate + UMP
about 105% activity compared to ADP
-
-
?
additional information
?
-
-
no activity with ATP, diphosphate, or acetyl phosphate as phosphate donors, no activity with D-glucose as phosphate acceptor substrate
-
-
?
additional information
?
-
the enzyme from Methanococcus jannaschii also shows glucokinase activity, a bifunctional MjPFK/GK
-
-
-
additional information
?
-
-
the enzyme from Methanococcus jannaschii also shows glucokinase 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-terminal, 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-terminal, 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-terminal, 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-terminal, 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-terminal, 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% activity compared to the activity with D-glucose and ADP: L-rhamnose, D-arabinose, D-lyxose, D-fucose, D-galactose, D-mannose, D-fructose, 2-deoxyglucose, D-glucosamine, D-xylose, maltose, lactose
-
-
?
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 glucokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional MevePFK/GK
-
-
-
additional information
?
-
the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional PFK/GK enzyme
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows glucokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows glucokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows glucokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows glucokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows glucokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
the enzyme from Methanosarcina mazei also shows glucokinase activity, a bifunctional MmazPFK/GK
-
-
-
additional information
?
-
the PFK from Pyrococcus horikoshii (PhPFK) has no activity with glucose
-
-
-
additional information
?
-
the PFK from Pyrococcus horikoshii (PhPFK) has no activity with glucose
-
-
-
additional information
?
-
the enzyme prefers ADP as phosphoryl donor, but ADP can be replaced by ATP resulting in a 5fold lower activity. The enzyme catalyzes the phosphorylation of fructose 6-phosphate and dephosphorylation of fructose 1,6-bisphosphate. In addition, it is able to phosphorylate D-glucose and nucleosides but with a much lower rate compared to that of fructose 6-phosphate, the enzyme shows 450fold lower activity with D-glucose (cf. EC 2.7.1.147) compared to that with fructose 6-phosphate. Only 20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP. No significant activity is detected in the presence of other phosphoryl donors examined. For the phosphoryl acceptor specificity, a number of alternative substrates including nucleosides, sugars and sugar phosphates are examined. Among the nucleoside substrates, adenosine shows 12%, 2-deoxyadenosine 17.5%, and thymidine 18% consumption of ADP. Among sugars and sugar phosphates, 22% and 5% relative activities can be observed with glucose and ribose 5-phosphate, respectively. Substrate specificity, overview
-
-
-
additional information
?
-
-
the enzyme prefers ADP as phosphoryl donor, but ADP can be replaced by ATP resulting in a 5fold lower activity. The enzyme catalyzes the phosphorylation of fructose 6-phosphate and dephosphorylation of fructose 1,6-bisphosphate. In addition, it is able to phosphorylate D-glucose and nucleosides but with a much lower rate compared to that of fructose 6-phosphate, the enzyme shows 450fold lower activity with D-glucose (cf. EC 2.7.1.147) compared to that with fructose 6-phosphate. Only 20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP. No significant activity is detected in the presence of other phosphoryl donors examined. For the phosphoryl acceptor specificity, a number of alternative substrates including nucleosides, sugars and sugar phosphates are examined. Among the nucleoside substrates, adenosine shows 12%, 2-deoxyadenosine 17.5%, and thymidine 18% consumption of ADP. Among sugars and sugar phosphates, 22% and 5% relative activities can be observed with glucose and ribose 5-phosphate, respectively. Substrate specificity, overview
-
-
-
additional information
?
-
the enzyme prefers ADP as phosphoryl donor, but ADP can be replaced by ATP resulting in a 5fold lower activity. The enzyme catalyzes the phosphorylation of fructose 6-phosphate and dephosphorylation of fructose 1,6-bisphosphate. In addition, it is able to phosphorylate D-glucose and nucleosides but with a much lower rate compared to that of fructose 6-phosphate, the enzyme shows 450fold lower activity with D-glucose (cf. EC 2.7.1.147) compared to that with fructose 6-phosphate. Only 20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP. No significant activity is detected in the presence of other phosphoryl donors examined. For the phosphoryl acceptor specificity, a number of alternative substrates including nucleosides, sugars and sugar phosphates are examined. Among the nucleoside substrates, adenosine shows 12%, 2-deoxyadenosine 17.5%, and thymidine 18% consumption of ADP. Among sugars and sugar phosphates, 22% and 5% relative activities can be observed with glucose and ribose 5-phosphate, respectively. Substrate specificity, overview
-
-
-
additional information
?
-
the enzyme prefers ADP as phosphoryl donor, but ADP can be replaced by ATP resulting in a 5fold lower activity. The enzyme catalyzes the phosphorylation of fructose 6-phosphate and dephosphorylation of fructose 1,6-bisphosphate. In addition, it is able to phosphorylate D-glucose and nucleosides but with a much lower rate compared to that of fructose 6-phosphate, the enzyme shows 450fold lower activity with D-glucose (cf. EC 2.7.1.147) compared to that with fructose 6-phosphate. Only 20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP. No significant activity is detected in the presence of other phosphoryl donors examined. For the phosphoryl acceptor specificity, a number of alternative substrates including nucleosides, sugars and sugar phosphates are examined. Among the nucleoside substrates, adenosine shows 12%, 2-deoxyadenosine 17.5%, and thymidine 18% consumption of ADP. Among sugars and sugar phosphates, 22% and 5% relative activities can be observed with glucose and ribose 5-phosphate, respectively. Substrate specificity, overview
-
-
-
additional information
?
-
-
the enzyme also shows glucokinase activity, a bifunctional AncPFK/GK ancestor enzyme
-
-
-
additional information
?
-
-
the enzyme from Methanosarcina mazei also shows glucokinase activity, a bifunctional AncMsPFK/GK
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
-
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
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
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
key enzyme of the glycolytic pathway
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
key enzyme of the glycolytic pathway
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
ir
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
r
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
?
ADP + D-fructose 6-phosphate
AMP + D-fructose 1,6-bisphosphate
-
-
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
-
-
-
r
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
-
ADP can be replaced by GDP and CDP to a limited extent
-
-
?
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
ADP can be replaced by acetylphosphate
-
-
?
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
ADP can be replaced by acetylphosphate
-
-
ir
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
-
ADP can be replaced by GDP, ATP and GTP to a limited extent
-
-
?
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
-
ADP can be replaced by GDP, ATP and GTP to a limited extent
-
-
ir
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
-
-
-
-
r
D-fructose 6-phosphate + ADP
D-fructose 1,6-bisphosphate + AMP
-
-
-
r
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CaCl2
2 mM ADP and 2 mM D-fructose 6-phosphate, CaCl2 show the lowest activity with 75% of the activity measured in the presence of MgCl2, activity does not change with the cation concentration in the range of 2.5 to 7 mM
Fe2+
-
16% of activity with Mg2+
MgSO4
2 mM ADP and 2 mM D-fructose 6-phosphate, magnesium is tested with 2 counter ions to discard any effect of the anion
MnCl2
2 mM ADP and 2 mM D-fructose 6-phosphate, increase in enzyme activity with the increase in MnCl2 concentration from 2.5 to 7 mM is observed
NiSO4
2 mM ADP and 2 mM D-fructose 6-phosphate, highest PhPFK activity is obtained with NiSO4 (97 units/mg), decrease in enzyme activity with the increase in MnCl2 concentration from 2.5 to 7 mM is observed
ZnCl2
2 mM ADP and 2 mM D-fructose 6-phosphate, no significant activity
Ca2+
-
-
Ca2+
activity is highest in the presence of CaCl2, followed by MgCl2, Co2+ and Mn2+
Co2+
-
30% of activity with Mg2+
Co2+
activity is highest in the presence of CaCl2, followed by MgCl2, Co2+ and Mn2+
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 70% of the activity with Mg2+
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+
best activating divalent cation
Co2+
metal-ion dependent enzyme, highest activity (5.09 mM/min*mg) in presence of Co2+ followed by Mg2+ (3.28 mM/min*mg) at 90°C and pH 7.5
KCl
activates at up to 0.5 M, inhibitory above about 1.0 M
KCl
-
has no evident effect on the AncMsPFK/GK activity
Mg2+
-
most efficient divalent cation, can be replaced by Ni2+, Co2+, and Mn2+
Mg2+
activity is highest in the presence of CaCl2, followed by MgCl2, Co2+ and Mn2+
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+
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+
-
required for activity
Mg2+
activates to 64% compared to Co2+
Mg2+
metal-ion dependent enzyme, highest activity (5.09 mM/min*mg) in presence of Co2+ followed by Mg2+ (3.28 mM/min*mg) at 90°C and pH 7.5
Mg2+
-
required for activity
Mn2+
-
62% of activity with Mg2+
Mn2+
activity is highest in the presence of CaCl2, followed by MgCl2, Co2+ and Mn2+
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 25% of the activity with Mg2+
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+
activates to 64% compared to Co2+
Mn2+
dependent on divalent metal cations. Highest activity in the presence of Co2+ (100%) followed by Mg2+ (64%), Mn2+ (64%) and Ni2+ (34%)
Ni2+
-
33% of activity with Mg2+
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+
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+
highest activity in the presence of 2.5 mM NiSO4
Ni2+
activates to 34% compared to Co2+
Ni2+
dependent on divalent metal cations. Highest activity in the presence of Co2+ (100%) followed by Mg2+ (64%), Mn2+ (64%) and Ni2+ (34%)
additional information
-
divalent cations are required for activity, Zn2+, Ca2+, and Cu2+ are poor metal cofactors
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
poor activation by Ca2+ probably due to steric hindrance
additional information
-
no significant activity is detected in the presence of Zn2+
additional information
no significant activity is detected in the presence of Zn2+
additional information
-
divalent cation is strictly required for activity, the true substrate seems to be the metal-nucleotide complex. The enzyme is promiscuous in relation to its metal usage where the only considerations for metal assisted catalysis seem to be related to the ionic radii and coordination geometry of the cations. The metal cation is bound to the highly conserved NXXE motif, which constitutes one of the signatures of the ribokinase superfamily. The binding of a second metal to the enzyme produces a complex with a reduced catalytic constant
additional information
the phosphofructokinase activity of the enzyme is metal ion-dependent, the highest activity is found in the presence of Co2+, followed by Mg2+ at 90°C and pH 7.5. 18% of maximal activity is shown in absence of metal ions
additional information
-
the phosphofructokinase activity of the enzyme is metal ion-dependent, the highest activity is found in the presence of Co2+, followed by Mg2+ at 90°C and pH 7.5. 18% of maximal activity is shown in absence of metal ions
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metabolism
Embden-Meyerhof glycolytic pathway, early step
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. 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. 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. Analsis of enzyme ADP-PFK structure (PDB ID 1U2X) from Pyrococcus furiosus. Sequences and structures comparisons. Pyrococcus horikoshii posseses a phosphofructokinase and a glucokinase
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 possesses 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 possesses 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. 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. 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 possesses 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 possesses 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 possesses 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. 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. 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. 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. Analsis of enzyme ADP-PFK structure (PDB ID 1U2X) from Pyrococcus furiosus. Sequences and structures comparisons. Pyrococcus horikoshii posseses a phosphofructokinase and a glucokinase
-
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. 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. 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. 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 possesses 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. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities
-
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
key enzyme of the modified Embden-Meyerhof pathway of heterotrophic and chemolithoautotrophic archaea
physiological function
the phosphofructokinase activity of the enzyme is not allosterically regulated
physiological function
-
the phosphofructokinase activity of the enzyme is not allosterically regulated
-
physiological function
-
key enzyme of the modified Embden-Meyerhof pathway of heterotrophic and chemolithoautotrophic archaea
-
physiological function
-
the phosphofructokinase activity of the enzyme is not allosterically regulated
-
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
-
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
-
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. 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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Kengen, S.W.M.; Tuininga, J.E.; Verhees, C.H.; Van der Oost, J.; Stams, A.J.M.; De Vos, W.M.
ADP-dependent glucokinase and phosphofructokinase from Pyrococcus furiosus
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Pyrococcus furiosus
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ADP-dependent glucokinase/phosphofructokinase, a novel bifunctional enzyme from the hyperthermophilic archaeon Methanococcus jannaschii
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Methanocaldococcus jannaschii
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Tuininga, J.E.; Verhees, C.H.; van der Oost, J.; Kengen, S.W.; Stams, A.J.; de Vos, W.M.
Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus
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Pyrococcus furiosus
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Ronimus, R.S.; Koning, J.; Morgan, H.W.
Purification and characterization of an ADP-dependent phosphofructokinase from Thermococcus zilligii
Extremophiles
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Thermococcus zilligii
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Verhees, C.H.; Tuininga, J.E.; Kengen, S.W.; Stams, A.J.; van der Oost, J.; de Vos, W.M.
ADP-dependent phosphofructokinases in mesophilic and thermophilic methanogenic archaea
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Methanocaldococcus jannaschii, Methanocaldococcus jannaschii (Q58999), Methanocaldococcus jannaschii DSM 2661 (Q58999)
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Ronimus, R.S.; de Heus, E.; Morgan, H.W.
Sequencing, expression, characterization and phylogeny of the ADP-dependent phosphofructokinase from the hyperthermophilic, euryarchaeal Thermococcus zilligii
Biochim. Biophys. Acta
1517
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2001
Thermococcus zilligii (Q9HH12), Thermococcus zilligii
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Jeong, J.J.; Fushinobu, S.; Ito, S.; Shoun, H.; Wakagi, T.
Archaeal ADP-dependent phosphofructokinase: expression, purification, crystallization and preliminary crystallographic analysis
Acta Crystallogr. Sect. D
59
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Thermococcus litoralis (Q977Q3), Thermococcus litoralis
brenda
Hansen, T.; Schonheit, P.
ADP-dependent 6-phosphofructokinase, an extremely thermophilic, non-allosteric enzyme from the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324
Extremophiles
8
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2004
Archaeoglobus fulgidus
brenda
Merino, F.; Guixe, V.
Specificity evolution of the ADP-dependent sugar kinase family: in silico studies of the glucokinase/phosphofructokinase bifunctional enzyme from Methanocaldococcus jannaschii
FEBS J.
275
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Methanocaldococcus jannaschii
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Currie, M.A.; Merino, F.; Skarina, T.; Wong, A.H.; Singer, A.; Brown, G.; Savchenko, A.; Caniuguir, A.; Guixe, V.; Yakunin, A.F.; Jia, Z.
ADP-dependent 6-phosphofructokinase from Pyrococcus horikoshii OT3: structure determination and biochemical characterization of PH1645
J. Biol. Chem.
284
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2009
Pyrococcus horikoshii, Pyrococcus horikoshii (O59355), Pyrococcus horikoshii OT-3 (O59355)
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Labes, A.; Schoenheit, P.
Sugar utilization in the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324: starch degradation to acetate and CO2 via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
Arch. Microbiol.
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2001
Archaeoglobus fulgidus, Archaeoglobus fulgidus 7324
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Merino, F.; Rivas-Pardo, J.A.; Caniuguir, A.; Garcia, I.; Guixe, V.
Catalytic and regulatory roles of divalent metal cations on the phosphoryl-transfer mechanism of ADP-dependent sugar kinases from hyperthermophilic archaea
Biochimie
94
516-524
2012
Pyrococcus horikoshii
brenda
Kengen, S.W.; de Bok, F.A.; van Loo, N.D.; Dijkema, C.; Stams, A.J.; de Vos, W.M.
Evidence for the operation of a novel Embden-Meyerhof pathway that involves ADP-dependent kinases during sugar fermentation by Pyrococcus furiosus
J. Biol. Chem.
269
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1994
Pyrococcus furiosus
brenda
Castro-Fernandez, V.; Bravo-Moraga, F.; Herrera-Morande, A.; Guixe, V.
Bifunctional ADP-dependent phosphofructokinase/glucokinase activity in the order Methanococcales - biochemical characterization of the mesophilic enzyme from Methanococcus maripaludis
FEBS J.
281
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2014
Methanococcus maripaludis (Q6LXQ3)
brenda
Zamora, R.; Gonzalez-rdenes, F.; Castro-Fernndez, V.; Guix, V.
ADP-dependent phosphofructokinases from the archaeal order Methanosarcinales display redundant glucokinase activity
Arch. Biochem. Biophys.
633
85-92
2017
Methanohalobium evestigatum (D7E8P3), Methanococcoides burtonii (Q12WB9), Methanococcoides burtonii OCM 468 (Q12WB9), Methanococcoides burtonii ACE-M (Q12WB9), Methanococcoides burtonii NBRC 107633 (Q12WB9), Methanohalobium evestigatum DSM 3721 (D7E8P3), Methanohalobium evestigatum OCM 161 (D7E8P3), Methanohalobium evestigatum Z-7303 (D7E8P3), Methanohalobium evestigatum ATCC BAA-1072 (D7E8P3), Methanohalobium evestigatum NBRC 107634 (D7E8P3), Methanococcoides burtonii DSM 6242 (Q12WB9)
brenda
Gonzalez-Ordenes, F.; Cea, P.A.; Fuentes-Ugarte, N.; Munoz, S.M.; Zamora, R.A.; Leonardo, D.; Garratt, R.C.; Castro-Fernandez, V.; Guixe, V.
ADP-dependent kinases from the archaeal order Methanosarcinales adapt to salt by a non-canonical evolutionarily conserved strategy
Front. Microbiol.
9
1305
2018
uncultured bacterium, Methanohalobium evestigatum (D7E8P3), Pyrococcus horikoshii (O59355), Methanosarcina mazei (Q8PZL9), Methanosarcina mazei OCM 88 (Q8PZL9), Methanosarcina mazei DSM 3647 (Q8PZL9), Methanosarcina mazei Goe1 (Q8PZL9), Methanosarcina mazei JCM 11833 (Q8PZL9), Methanohalobium evestigatum DSM 3721 (D7E8P3), Methanohalobium evestigatum OCM 161 (D7E8P3), Pyrococcus horikoshii ATCC 700860 (O59355), Methanohalobium evestigatum Z-7303 (D7E8P3), Methanohalobium evestigatum ATCC BAA-1072 (D7E8P3), Methanohalobium evestigatum NBRC 107634 (D7E8P3), Methanosarcina mazei ATCC BAA-159 (Q8PZL9)
brenda
Castro-Fernandez, V.; Herrera-Morande, A.; Zamora, R.; Merino, F.; Gonzalez-Ordenes, F.; Padilla-Salinas, F.; Pereira, H.M.; Brandao-Neto, J.; Garratt, R.C.; Guixe, V.
Reconstructed ancestral enzymes reveal that negative selection drove the evolution of substrate specificity in ADP-dependent kinases
J. Biol. Chem.
292
15598-15610
2017
uncultured bacterium, Pyrococcus horikoshii (O59355), Methanocaldococcus jannaschii (Q58999), Pyrococcus horikoshii ATCC 700860 (O59355)
brenda
Shakir, N.; Bibi, T.; Aslam, M.; Rashid, N.
Biochemical characterization of a highly active ADP-dependent phosphofructokinase from Thermococcus kodakarensis
J. Biosci. Bioeng.
129
6-15
2020
Thermococcus kodakarensis (Q5JD05), Thermococcus kodakarensis, Thermococcus kodakarensis JCM 12380 (Q5JD05), Thermococcus kodakarensis ATCC BAA-918 (Q5JD05)
brenda