2.7.1.147: ADP-specific glucose/glucosamine kinase
This is an abbreviated version!
For detailed information about ADP-specific glucose/glucosamine kinase, go to the full flat file.
Word Map on EC 2.7.1.147
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2.7.1.147
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hyperthermophilic
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thermococcus
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embden-meyerhof
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litoralis
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phosphofructokinases
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jannaschii
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furiosus
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glucokinases
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ribokinase
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methanococcales
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thermococcales
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6-phosphofructokinase
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hexokinases
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atp-pfks
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methanosarcinales
- 2.7.1.147
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hyperthermophilic
- thermococcus
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embden-meyerhof
- litoralis
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phosphofructokinases
- jannaschii
- furiosus
- glucokinases
- ribokinase
- methanococcales
- thermococcales
- 6-phosphofructokinase
- hexokinases
- atp-pfks
- methanosarcinales
Reaction
Synonyms
ADP-dependent glucokinase, ADP-dependent hexokinase, ADP-dependent kinase, ADP-GK, ADP-HK, ADP-Pfk, ADP-specific glucokinase, ADP:D-glucose 6-phosphotransferase, ADPGK, ancGK/PFK, AncMsPFK/GK, bifunctional ADP-dependent phosphofructokinase/glucokinase, GlcN kinase, glucosamine kinase, MevePFK/GK, MjPFK/GK, MmazPFK/GK, MmPFK/GK, More, NagC4, pfGK, pfkC, PhPFK, TK1110, tlGK
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Substrates Products
Substrates Products on EC 2.7.1.147 - ADP-specific glucose/glucosamine kinase
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REACTION DIAGRAM
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
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ir
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
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?
CDP + D-glucose
CMP + D-glucose 6-phosphate
12% of the activity with ADP
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?
TDP + D-glucose
TMP + D-glucose 6-phosphate
about 10% compared to the activity with ADP
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r
AMP + D-fructose 6-phosphate
10% of the activity with D-glucose
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?
ADP + D-fructose
AMP + D-fructose 6-phosphate
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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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AMP + D-glucosamine 6-phosphate
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the enzyme is highly specific for both substrates
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ADP + D-glucosamine
AMP + D-glucosamine 6-phosphate
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the enzyme is highly specific for both substrates
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r
ADP + D-glucosamine
AMP + D-glucosamine 6-phosphate
the enzyme functions as the glucosamine kinase responsible for the chitin degradation
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?
ADP + D-glucosamine
AMP + D-glucosamine 6-phosphate
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?
ADP + D-glucosamine
AMP + D-glucosamine 6-phosphate
the enzyme functions as the glucosamine kinase responsible for the chitin degradation
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AMP + D-glucose 6-phosphate
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first step of the Embden-Meyerhoff pathway
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ADP + D-glucose
AMP + D-glucose 6-phosphate
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the enzyme is highly specific for both substrates
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ADP + D-glucose
AMP + D-glucose 6-phosphate
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the enzyme is involved in the modified Embden-Meyerhof pathway
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ADP + D-glucose
AMP + D-glucose 6-phosphate
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diphosphate and ATP do not serve as phosphoryl donor
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ADP + D-glucose
AMP + D-glucose 6-phosphate
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first step of the Embden-Meyerhoff pathway
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r
ADP + D-glucose
AMP + D-glucose 6-phosphate
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the enzyme is highly specific for both substrates
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ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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enzyme shows substrate inhibition at high glucose concentrations
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
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
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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
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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
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ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
best substrate concentration is 0.35 mM glucose, high concentrations are inhibitory
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
step of the Embden-Meyerhoff pathway
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
substrate binding site structure, glucose-induced conformational change and domain closure in the enzyme
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ADP + D-glucose
AMP + D-glucose 6-phosphate
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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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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
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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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?
ADP + D-glucose
AMP + D-glucose 6-phosphate
catalysis follows a sequential ordered mechanism
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ADP + D-glucose
AMP + D-glucose 6-phosphate
catalysis follows a sequential ordered mechanism
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AMP + D-mannose 6-phosphate
17% of the velocity with D-glucose
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ADP + D-mannose
AMP + D-mannose 6-phosphate
17% of the velocity with D-glucose
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ADP + D-mannose
AMP + D-mannose 6-phosphate
20% of the activity with D-glucose
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D-glucose 6-phosphate + AMP
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ADP can be replaced by GDP and CDP to a limited extent
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D-glucose + ADP
D-glucose 6-phosphate + AMP
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CDP shows comparable activity
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D-glucose + ADP
D-glucose 6-phosphate + AMP
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CDP shows comparable activity
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GDP + D-glucose
GMP + D-glucose 6-phosphate
about 10% compared to the activity with ADP
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GDP + D-glucose
GMP + D-glucose 6-phosphate
55% of the activity with ADP
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?
UMP + D-glucose 6-phosphate
about 20% compared to the activity with ADP
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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
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UDP + D-glucose
UMP + D-glucose 6-phosphate
about 20% of the activity with ADP
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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
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additional information
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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
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additional information
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enzyme effectively utilizes glucose and cannot efficiently catalyze mannose, and 2-deoxyglucose. No activity with ATP, CTP, GTP, phosphoenolpyruvate
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additional information
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enzyme effectively utilizes glucose and cannot efficiently catalyze mannose, and 2-deoxyglucose. No activity with ATP, CTP, GTP, phosphoenolpyruvate
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additional information
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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
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additional information
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the enzyme from Methanococcus jannaschii also shows phosphofructokinase activity, a bifunctional MjPFK/GK
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additional information
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the enzyme from Methanococcus jannaschii also shows phosphofructokinase activity, a bifunctional MjPFK/GK
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
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additional information
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
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additional information
?
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
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additional information
?
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
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additional information
?
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
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additional information
?
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
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additional information
?
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
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additional information
?
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
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additional information
?
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
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additional information
?
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
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additional information
?
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
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-
additional information
?
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional MevePFK/GK
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additional information
?
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the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme
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additional information
?
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the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
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additional information
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the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
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additional information
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the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
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additional information
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the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
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additional information
?
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the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
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additional information
?
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the enzyme from Methanosarcina mazei also shows phosphofructokinase activity, a bifunctional MmazPFK/GK
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additional information
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no activity with ATP, GTP, CTP, UTP, TTP, diphosphate, polyphosphate, TDP, UDP, acetyl-phosphate, phosphoarginine, carbamoyl phosphate, phosphocreatine, and phosphoenolpyruvate as phosphoryl donors
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?
additional information
?
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no activity with ATP, GTP, CTP, UTP, TTP, diphosphate, polyphosphate, TDP, UDP, acetyl-phosphate, phosphoarginine, carbamoyl phosphate, phosphocreatine, and phosphoenolpyruvate as phosphoryl donors
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?
additional information
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substrate-induced fit, binding of ADP induces large conformational changes
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additional information
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substrate-induced fit, binding of ADP induces large conformational changes
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additional information
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activity is not observed toward chitobiose and N-,N-diacetylchitobiose
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additional information
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activity is not observed toward chitobiose and N-,N-diacetylchitobiose
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additional information
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catalysis follows a sequential ordered mechanism
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additional information
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catalysis follows a sequential ordered mechanism
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additional information
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the glucokinase from Thermococcus litoralis shows no activity with fructose 6-phosphate
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additional information
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the glucokinase from Thermococcus litoralis shows no activity with fructose 6-phosphate
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additional information
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catalysis follows a sequential ordered mechanism
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additional information
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the enzyme also shows phosphofructokinase activity, a bifunctional AncMsPFK/GK ancestor enzyme
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additional information
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the enzyme also shows phosphofructokinase activity, a bifunctional AncPFK/GK ancestor enzyme
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