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Literature summary for 2.7.1.146 extracted from
- Biochemical characterization of a highly active ADP-dependent phosphofructokinase from Thermococcus kodakarensis (2020), J. Biosci. Bioeng., 129, 6-15 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| phosphoenol pyruvate | slight activation | Thermococcus kodakarensis |  |
| phosphoenol pyruvate | slightly enhances activity | Thermococcus kodakarensis | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Thermococcus kodakarensis |
| gene pfkC, sequence comparisons, recombinant expression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL as soluble and active enzyme | Thermococcus kodakarensis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| adenosine | slight inhibition | Thermococcus kodakarensis | |
| AMP | competitive | Thermococcus kodakarensis | |
| ATP | competitive | Thermococcus kodakarensis | |
| citrate | slight inhibition | Thermococcus kodakarensis | |
| EDTA | 5 mM, complete loss of activity | Thermococcus kodakarensis | |
| additional information | addition of pyruvate does not affect the activity | Thermococcus kodakarensis | |
| Zn2+ | slightly inhibitory | Thermococcus kodakarensis | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetic analysis of the phosphofructokinase activity, overview | Thermococcus kodakarensis | |
| 0.32 | - |
ADP | pH 7.5, 90°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 0.32 | - |
ADP | pH 7.5, 90°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 0.55 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 0.55 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, recombinant enzyme, in presence of Mg2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 0.58 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 0.58 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 0.7 | - |
D-fructose 1,6-bisphosphate | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 0.74 | - |
ADP | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 0.74 | - |
ADP | pH 7.5, 50°C, recombinant enzyme, in presence of Mg2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 0.74 | - |
D-fructose 6-phosphate | pH 7.5, 90°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 0.74 | - |
D-fructose 6-phosphate | pH 7.5, 90°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 0.86 | - |
ADP | pH 7.5, 50°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 0.86 | - |
ADP | pH 7.5, 50°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 1.57 | - |
AMP | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 90 | - |
D-glucose | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 90 | - |
D-glucose | pH 7.5, 50°C, recombinant enzyme, in presence of Mg2+, substrates ADP and D-glucose | Thermococcus kodakarensis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | slight activation | Thermococcus kodakarensis | |
| Cd2+ | slight activation | Thermococcus kodakarensis | |
| Co2+ | best activating divalent cation | Thermococcus kodakarensis | |
| 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 | Thermococcus kodakarensis | |
| Mg2+ | activates to 64% compared to Co2+ | Thermococcus kodakarensis | |
| 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 | Thermococcus kodakarensis | |
| Mn2+ | activates to 64% compared to Co2+ | Thermococcus kodakarensis | |
| Mn2+ | dependent on divalent metal cations. Highest activity in the presence of Co2+ (100%) followed by Mg2+ (64%), Mn2+ (64%) and Ni2+ (34%) | Thermococcus kodakarensis | |
| 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 | Thermococcus kodakarensis | |
| Ni2+ | activates to 34% compared to Co2+ | Thermococcus kodakarensis | |
| Ni2+ | dependent on divalent metal cations. Highest activity in the presence of Co2+ (100%) followed by Mg2+ (64%), Mn2+ (64%) and Ni2+ (34%) | Thermococcus kodakarensis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 52000 | - |
SDS-PAGE | Thermococcus kodakarensis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + D-fructose 1,6-bisphosphate | Thermococcus kodakarensis | - |
ATP + D-fructose 6-phosphate | - |
r | |
| ADP + D-fructose 6-phosphate | Thermococcus kodakarensis | - |
AMP + D-fructose 1,6-bisphosphate | - |
r | |
| ADP + D-fructose 6-phosphate | Thermococcus kodakarensis JCM 12380 | - |
AMP + D-fructose 1,6-bisphosphate | - |
r | |
| ADP + D-fructose 6-phosphate | Thermococcus kodakarensis ATCC BAA-918 | - |
AMP + D-fructose 1,6-bisphosphate | - |
r | |
| ATP + D-fructose 6-phosphate | Thermococcus kodakarensis | - |
ADP + D-fructose 1,6-bisphosphate | - |
r | |
| ATP + D-fructose 6-phosphate | Thermococcus kodakarensis JCM 12380 | - |
ADP + D-fructose 1,6-bisphosphate | - |
r | |
| ATP + D-fructose 6-phosphate | Thermococcus kodakarensis ATCC BAA-918 | - |
ADP + D-fructose 1,6-bisphosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermococcus kodakarensis | Q5JD05 | - |
- |
| Thermococcus kodakarensis | Q5JD05 | Pyrococcus kodakaraensis strain KOD1 | - |
| Thermococcus kodakarensis ATCC BAA-918 | Q5JD05 | - |
- |
| Thermococcus kodakarensis ATCC BAA-918 | Q5JD05 | Pyrococcus kodakaraensis strain KOD1 | - |
| Thermococcus kodakarensis JCM 12380 | Q5JD05 | Pyrococcus kodakaraensis strain KOD1 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermococcus kodakarensis |
| recombinant enzyme 3.5fold from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by heat treatment at 80°C for 30 min, anion exchange chromatography, and dialysis, followed by hydrophobic interaction chromatography, and again dialysis | Thermococcus kodakarensis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 5.09 | - |
substrate: , pH 7.5, 50°C | Thermococcus kodakarensis |
| 19.5 | - |
purified recombinant enzyme, pH 7.5, 50°C, in presence of Co2+, substrates ADP and ribose 5-phosphate | Thermococcus kodakarensis |
| 19.5 | - |
substrate: ribose 5-phosphate, pH 7.5, 50°C | Thermococcus kodakarensis |
| 46 | - |
purified recombinant enzyme, pH 7.5, 50°C, in presence of Co2+, substrates ADP and adenosine | Thermococcus kodakarensis |
| 46 | - |
substrate: adenosine, pH 7.5, 50°C | Thermococcus kodakarensis |
| 66 | - |
purified recombinant enzyme, pH 7.5, 50°C, in presence of Co2+, substrates ADP and 2-deoxyadenosine | Thermococcus kodakarensis |
| 66 | - |
substrate: 2-deoxyadenosine, pH 7.5, 50°C | Thermococcus kodakarensis |
| 70 | - |
purified recombinant enzyme, pH 7.5, 50°C, in presence of Co2+, substrates ADP and thymidine | Thermococcus kodakarensis |
| 70 | - |
substrate: thymidine, pH 7.5, 50°C | Thermococcus kodakarensis |
| 86 | - |
purified recombinant enzyme, pH 7.5, 50°C, in presence of Co2+, substrates ADP and D-glucose, reaction of EC 2.7.1.147 | Thermococcus kodakarensis |
| 86 | - |
substrate: D-glucose, pH 7.5, 50°C | Thermococcus kodakarensis |
| 3280 | - |
purified recombinant enzyme, pH 7.5, 50°C, in presence of Mg2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis |
| 5090 | - |
purified recombinant enzyme, pH 7.5, 50°C, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + 2'-deoxyadenosine | - |
Thermococcus kodakarensis | AMP + ? | - |
? | |
| ADP + 2'-deoxyadenosine | - |
Thermococcus kodakarensis | AMP + dAMP | - |
r | |
| ADP + adenosine | - |
Thermococcus kodakarensis | 2 AMP | - |
r | |
| ADP + adenosine | - |
Thermococcus kodakarensis | AMP + ? | - |
? | |
| ADP + D-fructose 1,6-bisphosphate | - |
Thermococcus kodakarensis | ATP + D-fructose 6-phosphate | - |
r | |
| ADP + D-fructose 6-phosphate | - |
Thermococcus kodakarensis | AMP + D-fructose 1,6-bisphosphate | - |
r | |
| ADP + D-fructose 6-phosphate | the rate of dephosphorylation of fructose 1,6-bisphosphate is 3times lower at 50°C than the phosphorylation of fructose 6-phosphate | Thermococcus kodakarensis | AMP + D-fructose 1,6-bisphosphate | - |
r | |
| ADP + D-fructose 6-phosphate | - |
Thermococcus kodakarensis JCM 12380 | AMP + D-fructose 1,6-bisphosphate | - |
r | |
| ADP + D-fructose 6-phosphate | - |
Thermococcus kodakarensis ATCC BAA-918 | AMP + D-fructose 1,6-bisphosphate | - |
r | |
| ADP + D-glucose | - |
Thermococcus kodakarensis | AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | cf. EC 2.7.1.147 | Thermococcus kodakarensis | AMP + D-glucose 6-phosphate | - |
r | |
| ADP + ribose 5-phosphate | - |
Thermococcus kodakarensis | AMP + ? | - |
? | |
| ADP + ribose 5-phosphate | - |
Thermococcus kodakarensis | AMP + ribose 1,5-bisphosphate | - |
r | |
| ADP + thymidine | - |
Thermococcus kodakarensis | AMP + ? | - |
? | |
| ADP + thymidine | - |
Thermococcus kodakarensis | AMP + TMP | - |
r | |
| AMP + D-fructose 1,6-bisphosphate | - |
Thermococcus kodakarensis | ADP + D-fructose 6-phosphate | - |
r | |
| ATP + D-fructose 6-phosphate | - |
Thermococcus kodakarensis | ADP + D-fructose 1,6-bisphosphate | - |
r | |
| ATP + D-fructose 6-phosphate | 20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP | Thermococcus kodakarensis | ADP + D-fructose 1,6-bisphosphate | - |
r | |
| ATP + D-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 | Thermococcus kodakarensis | ADP + D-fructose 1,6-bisphosphate | - |
r | |
| ATP + D-fructose 6-phosphate | - |
Thermococcus kodakarensis JCM 12380 | ADP + D-fructose 1,6-bisphosphate | - |
r | |
| ATP + D-fructose 6-phosphate | 20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP | Thermococcus kodakarensis JCM 12380 | ADP + D-fructose 1,6-bisphosphate | - |
r | |
| ATP + D-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 | Thermococcus kodakarensis JCM 12380 | ADP + D-fructose 1,6-bisphosphate | - |
r | |
| ATP + D-fructose 6-phosphate | - |
Thermococcus kodakarensis ATCC BAA-918 | ADP + D-fructose 1,6-bisphosphate | - |
r | |
| ATP + D-fructose 6-phosphate | 20% phosphofructokinase activity is observed in the presence of 2 mM ATP compared to 100% in the presence of equimolar ADP | Thermococcus kodakarensis ATCC BAA-918 | ADP + D-fructose 1,6-bisphosphate | - |
r | |
| ATP + D-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 | Thermococcus kodakarensis ATCC BAA-918 | ADP + D-fructose 1,6-bisphosphate | - |
r | |
| 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 | Thermococcus kodakarensis | ? | - |
- |
|
| 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 | Thermococcus kodakarensis JCM 12380 | ? | - |
- |
|
| 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 | Thermococcus kodakarensis ATCC BAA-918 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 52000, SDS-PAGE | Thermococcus kodakarensis |
| ? | x * 52661, sequence calculation, x * 52000, recombinant enzyme, SDS-PAGE | Thermococcus kodakarensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADP-dependent phosphofructokinase | - |
Thermococcus kodakarensis |
| PFK | - |
Thermococcus kodakarensis |
| pfkC | - |
Thermococcus kodakarensis |
| TK0376 | locus name | Thermococcus kodakarensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 90 | - |
- |
Thermococcus kodakarensis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 100 | activity range, profile overview | Thermococcus kodakarensis |
| 70 | 100 | 70°C: about 45% of maximal activity, 100°C: about 75% of maximal activity | Thermococcus kodakarensis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
no significant difference activity after incubation of 180 min | Thermococcus kodakarensis |
| 80 | - |
purified enzyme, 180 min, completely stable | Thermococcus kodakarensis |
| 90 | - |
half-life: 120 min | Thermococcus kodakarensis |
| 90 | - |
purified enzyme, half life is 120 min | Thermococcus kodakarensis |
| 100 | - |
half-life: 30 min | Thermococcus kodakarensis |
| 100 | - |
purified enzyme, half life is 30 min | Thermococcus kodakarensis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 95 | - |
D-fructose 1,6-bisphosphate | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 104 | - |
D-glucose | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 104 | - |
D-glucose | pH 7.5, 50°C, recombinant enzyme, in presence of Mg2+, substrates ADP and D-glucose | Thermococcus kodakarensis | |
| 112 | - |
AMP | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 282 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 282 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, recombinant enzyme, in presence of Mg2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 338 | - |
ADP | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 338 | - |
ADP | pH 7.5, 50°C, recombinant enzyme, in presence of Mg2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 475 | - |
ADP | pH 7.5, 50°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 475 | - |
ADP | pH 7.5, 50°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 495 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 495 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 4238 | - |
D-fructose 6-phosphate | pH 7.5, 90°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 4328 | - |
D-fructose 6-phosphate | pH 7.5, 90°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 4410 | - |
ADP | pH 7.5, 90°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 4410 | - |
ADP | pH 7.5, 90°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
- |
Thermococcus kodakarensis |
| 7.5 | - |
assay at | Thermococcus kodakarensis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 9 | activity range, profile overview | Thermococcus kodakarensis |
| 6 | 8 | pH 6.0: about 80% of maximal activity, pH 8.0: about 45% of maximal activity | Thermococcus kodakarensis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ADP | - |
Thermococcus kodakarensis | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Thermococcus kodakarensis | sequence calculation | - |
6.71 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the phosphofructokinase activity of the enzyme is not allosterically regulated | Thermococcus kodakarensis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.16 | - |
D-glucose | pH 7.5, 50°C, recombinant enzyme, in presence of Mg2+, substrates ADP and D-glucose | Thermococcus kodakarensis | |
| 115 | - |
D-glucose | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 127 | - |
D-fructose 1,6-bisphosphate | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 138 | - |
ADP | pH 7.5, 90°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 456.8 | - |
ADP | pH 7.5, 50°C, recombinant enzyme, in presence of Mg2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 457 | - |
ADP | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 512.7 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, recombinant enzyme, in presence of Mg2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 513 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 552 | - |
ADP | pH 7.5, 50°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 552 | - |
ADP | pH 7.5, 50°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 565 | - |
D-fructose 6-phosphate | pH 7.5, 90°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 713 | - |
AMP | pH 7.5, 50°C, 5 mM Mg2+ | Thermococcus kodakarensis | |
| 851 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, 5 mM Co2+ | Thermococcus kodakarensis | |
| 853.5 | - |
D-fructose 6-phosphate | pH 7.5, 50°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 5727 | - |
D-fructose 6-phosphate | pH 7.5, 90°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
| 13781 | - |
ADP | pH 7.5, 90°C, recombinant enzyme, in presence of Co2+, substrates ADP and D-fructose 6-phosphate | Thermococcus kodakarensis | |
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