EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.3.11 | expression in Escherichia coli | Pyrobaculum calidifontis |
3.1.3.11 | gene Pcal_0111, sequence comparisons, recombinant expression of mostly soluble enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL | Pyrobaculum calidifontis |
4.1.2.13 | expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL cells | Pyrobaculum calidifontis |
4.1.2.13 | expression in Escherichia coli | Pyrobaculum calidifontis |
4.1.2.13 | gene Pcal_0111, sequence comparisons, recombinant expression of mostly soluble enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL | Pyrobaculum calidifontis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.11 | ADP | 1.5 mM, 30% decrease in activity; 30% inhibition at 1.5 mM | Pyrobaculum calidifontis | |
3.1.3.11 | ATP | 1.5 mM, 90% decrease in activity; 90% inhibition at 1.5 mM | Pyrobaculum calidifontis | |
3.1.3.11 | EDTA | 5 mM, complete inhibition of phosphatase activity; complete inhibition of phosphatase activity by 5 mM EDTA | Pyrobaculum calidifontis | |
3.1.3.11 | additional information | no inhibition by AMP; no significant effect of AMP on the phosphatase activity | Pyrobaculum calidifontis | |
4.1.2.13 | ADP | - |
Pyrobaculum calidifontis | |
4.1.2.13 | ATP | - |
Pyrobaculum calidifontis | |
4.1.2.13 | additional information | the enzyme does not show any inhibition in the presence of 10 mM AMP | Pyrobaculum calidifontis | |
4.1.2.13 | Sodium borohydride | incubation with sodium borohydride in the presence of substrate results more than 80% of decrease in aldolase activity; more than 80% of decrease in aldolase activity in the presence of substrate. Negligible decrease in aldolase activity when Pcal_0111 and sodium borohydride are incubated in the absence of the substrate; results in more than 80% of decrease in aldolase activity of Pcal_0111 in the presence of substrate, also a negligible decrease in aldolase activity is observed when Pcal_0111 and sodium borohydride are incubated in the absence of the substrate | Pyrobaculum calidifontis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.11 | additional information | - |
additional information | Michaelis-Menten kinetics, from Arrhenius plots, activation energies for phosphatase and aldolase reactions are calculated 46.5 and 75.62 kJ/mol, respectively | Pyrobaculum calidifontis | |
3.1.3.11 | 0.059 | - |
D-fructose 1,6-bisphosphate | recombinant enzyme, pH 8.0, 55°C | Pyrobaculum calidifontis | |
3.1.3.11 | 0.06 | - |
D-fructose 1,6-bisphosphate | pH 8.0, 25°C | Pyrobaculum calidifontis | |
4.1.2.13 | additional information | - |
additional information | Michaelis-Menten kinetics, from Arrhenius plots, activation energies for phosphatase and aldolase reactions are calculated 46.5 and 75.62 kJ/mol, respectively | Pyrobaculum calidifontis | |
4.1.2.13 | 0.821 | - |
D-fructose 1,6-bisphosphate | pH 8.0, 25°C | Pyrobaculum calidifontis | |
4.1.2.13 | 0.822 | - |
D-fructose 1,6-bisphosphate | at pH 6.0 and 25°C | Pyrobaculum calidifontis | |
4.1.2.13 | 0.822 | - |
D-fructose 1,6-bisphosphate | recombinant enzyme, pH 8.0, 55°C | Pyrobaculum calidifontis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.11 | Mg2+ | activates highly, best at 2 mM MnCl2 | Pyrobaculum calidifontis | |
3.1.3.11 | Mg2+ | phosphatase activity is significantly increased in the presence of Mn2+ and Mg2+. In the presence of Mg2+ highest activity is found at 2 mM | Pyrobaculum calidifontis | |
3.1.3.11 | Mn2+ | activates 20fold, best at 0.1 mM MnCl2 | Pyrobaculum calidifontis | |
3.1.3.11 | Mn2+ | phosphatase activity is significantly increased in the presence of Mn2+ and Mg2+. 20fold increase in enzyme activity in the presence of 0.1 mM MnCl2 compared to control in which no metal ion is added. In the presence of Mn2+, the highest phosphatase activity is found at a final concentration of 0.1 mM | Pyrobaculum calidifontis | |
3.1.3.11 | additional information | residues involved in metal binding include Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 | Pyrobaculum calidifontis | |
4.1.2.13 | Mg2+ | activates | Pyrobaculum calidifontis | |
4.1.2.13 | Mn2+ | activates | Pyrobaculum calidifontis | |
4.1.2.13 | additional information | residues involved in metal binding include Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 | Pyrobaculum calidifontis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.1.3.11 | 44513 | - |
calculated from sequence | Pyrobaculum calidifontis |
4.1.2.13 | 44513 | - |
calculated from sequence | Pyrobaculum calidifontis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.11 | D-fructose 1,6-bisphosphate + H2O | Pyrobaculum calidifontis | - |
D-fructose 6-phosphate + phosphate | - |
? | |
3.1.3.11 | D-fructose 1,6-bisphosphate + H2O | Pyrobaculum calidifontis | key enzyme of the gluconeogenic pathway | D-fructose 6-phosphate + phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | Pyrobaculum calidifontis | - |
glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | Pyrobaculum calidifontis JCM 11548 | - |
glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | Pyrobaculum calidifontis VA1 | - |
glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | Pyrobaculum calidifontis JGM 11548 | - |
glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | Pyrobaculum calidifontis | - |
glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | Pyrobaculum calidifontis JCM 11548 | - |
glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | Pyrobaculum calidifontis VA1 | - |
glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | Pyrobaculum calidifontis JGM 11548 | - |
glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.11 | Pyrobaculum calidifontis | A3MSD2 | - |
- |
3.1.3.11 | Pyrobaculum calidifontis JCM 11548 | A3MSD2 | - |
- |
3.1.3.11 | Pyrobaculum calidifontis VA1 | A3MSD2 | - |
- |
4.1.2.13 | Pyrobaculum calidifontis | A3MSD2 | - |
- |
4.1.2.13 | Pyrobaculum calidifontis JCM 11548 | A3MSD2 | - |
- |
4.1.2.13 | Pyrobaculum calidifontis JGM 11548 | A3MSD2 | - |
- |
4.1.2.13 | Pyrobaculum calidifontis VA1 | A3MSD2 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.3.11 | - |
Pyrobaculum calidifontis |
3.1.3.11 | recombinant enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by heat treatment at 80°C for 25 min, nickel affinity chromatography, and dialysis | Pyrobaculum calidifontis |
4.1.2.13 | - |
Pyrobaculum calidifontis |
4.1.2.13 | Ni-NTA column chromatography | Pyrobaculum calidifontis |
4.1.2.13 | recombinant enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by heat treatment at 80°C for 25 min, nickel affinity chromatography, and dialysis | Pyrobaculum calidifontis |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.3.11 | additional information | the facultative aerobe that grows optimally at 90-95°C | Pyrobaculum calidifontis | - |
4.1.2.13 | additional information | the facultative aerobe that grows optimally at 90-95°C | Pyrobaculum calidifontis | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.1.3.11 | 4 | - |
pH 8.0, 25°C | Pyrobaculum calidifontis |
3.1.3.11 | 4.01 | 4.67 | purified recombinant enzyme, substrate D-fructose 1,6-bisphosphate, pH 8.0, 55°C | Pyrobaculum calidifontis |
4.1.2.13 | 1.3 | - |
pH 8.0, 25°C | Pyrobaculum calidifontis |
4.1.2.13 | 1.32 | - |
purified recombinant enzyme, substrate D-fructose 1,6-bisphosphate, pH 8.0, 55°C | Pyrobaculum calidifontis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.11 | 5-phospho-D-ribosyl diphosphate + H2O | 40.73% activity compared to D-fructose 1,6-bisphosphate | Pyrobaculum calidifontis | ? | - |
? | |
3.1.3.11 | D-fructose 1,6-bisphosphate + H2O | - |
Pyrobaculum calidifontis | D-fructose 6-phosphate + phosphate | - |
? | |
3.1.3.11 | D-fructose 1,6-bisphosphate + H2O | preferred substrate | Pyrobaculum calidifontis | D-fructose 6-phosphate + phosphate | - |
? | |
3.1.3.11 | D-fructose 1,6-bisphosphate + H2O | key enzyme of the gluconeogenic pathway | Pyrobaculum calidifontis | D-fructose 6-phosphate + phosphate | - |
? | |
3.1.3.11 | glyceraldehyde 3-phosphate + H2O | 11.43% of the activity compared to D-fructose 1,6-bisphosphate | Pyrobaculum calidifontis | ? | - |
? | |
3.1.3.11 | GTP + H2O | 22.9% of the activity compared to D-fructose 1,6-bisphosphate | Pyrobaculum calidifontis | ? | - |
? | |
3.1.3.11 | additional information | purified recombinant Pcal_0111 catalyzes both phosphatase and aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. Although the enzyme can utilize several substrates for dephosphorylation, no phosphatase activity is detected with AMP, UTP, NADP, glucose 6-phosphate, ribose 5-phosphate, riboflavin 5-monophosphate, and pyridoxal 5-phosphate. Varying amounts of phosphatase activity are found when ATP, GTP, ADP, CTP, glyceraldehyde 3-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, and phosphoribosyl diphosphate are used as substrates. The highest phosphatase activity is found with fructose 1,6-bisphosphate followed by phosphoribosyl diphosphate. Spectrophotometric coupled enzyme assay as discontinuous assay method, or product phosphate detection by malachite green assay method. Substrate binding residues include Tyr229, Lys232, and Tyr358 | Pyrobaculum calidifontis | ? | - |
? | |
3.1.3.11 | additional information | no phosphatase activity could be detected with AMP, UTP, NADP, glucose 6-phosphate, ribose 5-phosphate, riboflavin 5-monophosphate, and pyridoxal 5-phosphate | Pyrobaculum calidifontis | ? | - |
- |
|
3.1.3.11 | phosphoribosyl diphosphate + H2O | 40.73% of the activity compared to D-fructose 1,6-bisphosphate | Pyrobaculum calidifontis | ? | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | - |
Pyrobaculum calidifontis | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | 100% activity | Pyrobaculum calidifontis | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | - |
Pyrobaculum calidifontis JCM 11548 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | 100% activity | Pyrobaculum calidifontis JCM 11548 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | - |
Pyrobaculum calidifontis VA1 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | 100% activity | Pyrobaculum calidifontis VA1 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | - |
Pyrobaculum calidifontis JGM 11548 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate | 100% activity | Pyrobaculum calidifontis JGM 11548 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | - |
Pyrobaculum calidifontis | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | preferred substrate | Pyrobaculum calidifontis | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | - |
Pyrobaculum calidifontis JCM 11548 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | preferred substrate | Pyrobaculum calidifontis JCM 11548 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | - |
Pyrobaculum calidifontis VA1 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | preferred substrate | Pyrobaculum calidifontis VA1 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | - |
Pyrobaculum calidifontis JGM 11548 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | D-fructose 1,6-bisphosphate + H2O | preferred substrate | Pyrobaculum calidifontis JGM 11548 | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? | |
4.1.2.13 | additional information | purified recombinant Pcal_0111 catalyzes both phosphatase and aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. Although the enzyme can utilize several substrates for dephosphorylation, no phosphatase activity is detected with AMP, UTP, NADP, glucose 6-phosphate, ribose 5-phosphate, riboflavin 5-monophosphate, and pyridoxal 5-phosphate. Varying amounts of phosphatase activity are found when ATP, GTP, ADP, CTP, glyceraldehyde 3-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, and phosphoribosyl diphosphate are used as substrates. Substrate binding residues include Tyr229, Lys232, and Tyr358 | Pyrobaculum calidifontis | ? | - |
? | |
4.1.2.13 | additional information | purified recombinant Pcal_0111 catalyzes both phosphatase and aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. Although the enzyme can utilize several substrates for dephosphorylation, no phosphatase activity is detected with AMP, UTP, NADP, glucose 6-phosphate, ribose 5-phosphate, riboflavin 5-monophosphate, and pyridoxal 5-phosphate. Varying amounts of phosphatase activity are found when ATP, GTP, ADP, CTP, glyceraldehyde 3-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, and phosphoribosyl diphosphate are used as substrates. Substrate binding residues include Tyr229, Lys232, and Tyr358 | Pyrobaculum calidifontis JCM 11548 | ? | - |
? | |
4.1.2.13 | additional information | purified recombinant Pcal_0111 catalyzes both phosphatase and aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. Although the enzyme can utilize several substrates for dephosphorylation, no phosphatase activity is detected with AMP, UTP, NADP, glucose 6-phosphate, ribose 5-phosphate, riboflavin 5-monophosphate, and pyridoxal 5-phosphate. Varying amounts of phosphatase activity are found when ATP, GTP, ADP, CTP, glyceraldehyde 3-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, and phosphoribosyl diphosphate are used as substrates. Substrate binding residues include Tyr229, Lys232, and Tyr358 | Pyrobaculum calidifontis VA1 | ? | - |
? | |
4.1.2.13 | additional information | purified recombinant Pcal_0111 catalyzes both phosphatase and aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. Although the enzyme can utilize several substrates for dephosphorylation, no phosphatase activity is detected with AMP, UTP, NADP, glucose 6-phosphate, ribose 5-phosphate, riboflavin 5-monophosphate, and pyridoxal 5-phosphate. Varying amounts of phosphatase activity are found when ATP, GTP, ADP, CTP, glyceraldehyde 3-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, and phosphoribosyl diphosphate are used as substrates. Substrate binding residues include Tyr229, Lys232, and Tyr358 | Pyrobaculum calidifontis JGM 11548 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.3.11 | ? | x * 44513, sequence calculation | Pyrobaculum calidifontis |
4.1.2.13 | ? | x * 44000, SDS-PAGE | Pyrobaculum calidifontis |
4.1.2.13 | ? | x * 44513, calculated from amino acid sequence | Pyrobaculum calidifontis |
4.1.2.13 | ? | x * 44513, sequence calculation | Pyrobaculum calidifontis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.3.11 | bifunctional fructose-1,6-bisphosphate aldolase/phosphatase | - |
Pyrobaculum calidifontis |
3.1.3.11 | fructose 1,6-bisphosphatase/aldolase | - |
Pyrobaculum calidifontis |
3.1.3.11 | fructose-1,6-bisphosphate aldolase/phosphatase | - |
Pyrobaculum calidifontis |
3.1.3.11 | More | cf. EC 4.1.2.13 | Pyrobaculum calidifontis |
3.1.3.11 | Pcal_0111 | - |
Pyrobaculum calidifontis |
4.1.2.13 | bifunctional fructose-1,6-bisphosphate aldolase/phosphatase | - |
Pyrobaculum calidifontis |
4.1.2.13 | fructose 1,6-bisphosphatase/aldolase | - |
Pyrobaculum calidifontis |
4.1.2.13 | fructose-1,6-bisphosphate aldolase/phosphatase | - |
Pyrobaculum calidifontis |
4.1.2.13 | More | cf. EC 3.1.3.11 | Pyrobaculum calidifontis |
4.1.2.13 | Pcal_0111 | - |
Pyrobaculum calidifontis |
4.1.2.13 | Pcal_0111 | bifunctional fructose-1,6-bisphosphate aldolase/phosphatase | Pyrobaculum calidifontis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.3.11 | 100 | - |
fructose 1,6-bisphosphatase, the enzyme activity increases linearly with the increase in temperature up to 100°C | Pyrobaculum calidifontis |
3.1.3.11 | 100 | - |
difference in optimal temperature of aldolase and phosphatase activity of the enzyme could be due to difference in heat stabilities of the substrates | Pyrobaculum calidifontis |
4.1.2.13 | 80 | - |
the enzyme denatures in the presence of ATP | Pyrobaculum calidifontis |
4.1.2.13 | 90 | - |
- |
Pyrobaculum calidifontis |
4.1.2.13 | 90 | - |
fructose 1,6-bisphosphate aldolase | Pyrobaculum calidifontis |
4.1.2.13 | 90 | - |
difference in optimal temperature of aldolase and phosphatase activity of the enzyme could be due to difference in heat stabilities of the substrates | Pyrobaculum calidifontis |
4.1.2.13 | 100 | - |
difference in optimal temperature of aldolase and phosphatase activity of the enzyme could be due to difference in heat stabilities of the substrates | Pyrobaculum calidifontis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.3.11 | 80 | - |
purified recombinant enzyme, 24 h, completely stable | Pyrobaculum calidifontis |
3.1.3.11 | 80 | - |
no significant change in activity even after 24 h. The enzyme denatures in the presence of ATP | Pyrobaculum calidifontis |
3.1.3.11 | 90 | 100 | purified recombinant enzyme, half-life is 120 min, no significant change in the circular dichroism spectra of the protein up to 90°C | Pyrobaculum calidifontis |
3.1.3.11 | 100 | - |
half-life: 120 min | Pyrobaculum calidifontis |
4.1.2.13 | 80 | - |
purified recombinant enzyme, 24 h, completely stable | Pyrobaculum calidifontis |
4.1.2.13 | 80 | - |
no significant change in activity even after 24 h. The enzyme denatures in the presence of ATP | Pyrobaculum calidifontis |
4.1.2.13 | 90 | 100 | purified recombinant enzyme, half-life is 120 min, no significant change in the circular dichroism spectra of the protein up to 90°C | Pyrobaculum calidifontis |
4.1.2.13 | 100 | - |
half-life: 120 min | Pyrobaculum calidifontis |
4.1.2.13 | 100 | - |
recombinant enzyme is highly stable with a half-life of 120 min at 100°C | Pyrobaculum calidifontis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.3.11 | 8 | - |
- |
Pyrobaculum calidifontis |
3.1.3.11 | 8 | - |
phosphatase activity | Pyrobaculum calidifontis |
4.1.2.13 | 8 | - |
- |
Pyrobaculum calidifontis |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.1.3.11 | 7.5 | 10 | pH 7.5: about 50% of maximal activity, pH 10.0: about 40% of maximal activity | Pyrobaculum calidifontis |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
3.1.3.11 | Pyrobaculum calidifontis | sequence calculation | - |
6.16 |
3.1.3.11 | Pyrobaculum calidifontis | calculated from sequence | - |
6.16 |
4.1.2.13 | Pyrobaculum calidifontis | sequence calculation | - |
6.16 |
4.1.2.13 | Pyrobaculum calidifontis | calculated from sequence | - |
6.16 |
4.1.2.13 | Pyrobaculum calidifontis | calculated from amino acid sequence | - |
6.2 |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
3.1.3.11 | 0.75 | - |
pH 8.0, 25°C | Pyrobaculum calidifontis | ATP | |
3.1.3.11 | 0.75 | - |
recombinant enzyme, pH 8.0, 60°C | Pyrobaculum calidifontis | ATP | |
4.1.2.13 | 0.75 | - |
at pH 6.0 and 25°C | Pyrobaculum calidifontis | ATP |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.3.11 | evolution | the archaeal enzyme belongs to the class V of fructose-1, 6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases | Pyrobaculum calidifontis |
3.1.3.11 | metabolism | key enzyme of the gluconeogenic pathway | Pyrobaculum calidifontis |
3.1.3.11 | additional information | the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate | Pyrobaculum calidifontis |
4.1.2.13 | evolution | the archaeal enzyme belongs to the class V of fructose-1,6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases | Pyrobaculum calidifontis |
4.1.2.13 | additional information | the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate | Pyrobaculum calidifontis |