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Literature summary extracted from

  • Aziz, I.; Rashid, N.; Ashraf, R.; Bashir, Q.; Imanaka, T.; Akhtar, M.
    Pcal_0111, a highly thermostable bifunctional fructose-1,6-bisphosphate aldolase/phosphatase from Pyrobaculum calidifontis (2017), Extremophiles, 21, 513-521 .
    View publication on PubMed

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

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
-
-

Purification (Commentary)

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

Source Tissue

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
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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 ?
-
 ?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

pH Range

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

pI Value

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

IC50 Value

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

General Information

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