2.7.1.146: ADP-specific phosphofructokinase
This is an abbreviated version!
For detailed information about ADP-specific phosphofructokinase, go to the full flat file.
Word Map on EC 2.7.1.146
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2.7.1.146
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hyperthermophilic
-
embden-meyerhof
-
archaeon
-
methanococcus
-
jannaschii
-
amp
-
furiosus
-
thermococcus
-
atp-pfks
-
phosphofructokinases
-
ppi-dependent
-
fructose-1,6-bisphosphate
-
sulfate-reducing
-
archaeoglobus
-
fulgidus
-
pyrophosphate-dependent
-
zilligii
-
thermococcales
-
eucarya
-
horikoshii
-
adp-forming
- 2.7.1.146
-
hyperthermophilic
-
embden-meyerhof
- archaeon
-
methanococcus
- jannaschii
- amp
- furiosus
- thermococcus
- atp-pfks
-
phosphofructokinases
-
ppi-dependent
- fructose-1,6-bisphosphate
-
sulfate-reducing
-
archaeoglobus
- fulgidus
-
pyrophosphate-dependent
- zilligii
- thermococcales
- eucarya
- horikoshii
-
adp-forming
Reaction
Synonyms
ADP dependent phosphofructokinase, ADP-6-phosphofructokinase, ADP-dependent 6-phosphofructokinase, ADP-dependent glucokinase, ADP-dependent glucokinase/phosphofructokinase, ADP-dependent PFK, ADP-dependent phosphofructokinase, ADP-GK, ADP-Pfk, ancGK/PFK, AncMsPFK/GK, bifunctional ADP-dependent phosphofructokinase/glucokinase, MevePFK/GK, MJ1604, MjPFK/GK, MmazPFK/GK, MmPFK/GK, More, PFK, PFK-ADP, pfkC, PhPFK, TK0376, TLPFK
ECTree
2.7.1.146 ADP-specific phosphofructokinaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.7.1.146 - ADP-specific phosphofructokinase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + D-fructose 1,6-bisphosphate
ATP + D-fructose 6-phosphate
-
-
-
r
ADP + ribose 5-phosphate
AMP + ribose 1,5-bisphosphate
-
-
-
r
CDP + beta-D-fructose 6-phosphate
CMP + D-fructose 1,6-bisphosphate
about 15% compared to the activity with ADP
-
-
ir
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
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
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
-
-
-
