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Literature summary extracted from

  • Fukuda, W.; Fukui, T.; Atomi, H.; Imanaka, T.
    First characterization of an archaeal GTP-dependent phosphoenolpyruvate carboxykinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 (2004), J. Bacteriol., 186, 4620-4627.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.32 expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL Thermococcus kodakarensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.32 2-oxoglutarate weak inhibition Thermococcus kodakarensis
4.1.1.32 pyruvate weak inhibition Thermococcus kodakarensis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.32 0.018
-
 oxaloacetate 60°C, pH 7.0 Thermococcus kodakarensis
4.1.1.32 0.0181
-
 oxaloacetate pH 7.0, 60°C Thermococcus kodakarensis
4.1.1.32 0.0185
-
 GDP pH 7.0, 60°C Thermococcus kodakarensis
4.1.1.32 0.019
-
 GDP 60°C, pH 7.0 Thermococcus kodakarensis
4.1.1.32 0.036
-
 GTP 60°C, pH 7.0 Thermococcus kodakarensis
4.1.1.32 0.0361
-
 GTP pH 7.0, 60°C Thermococcus kodakarensis
4.1.1.32 0.0712
-
 IDP pH 7.0, 60°C Thermococcus kodakarensis
4.1.1.32 0.0715
-
 ITP pH 7.0, 60°C Thermococcus kodakarensis
4.1.1.32 0.131
-
 phosphoenolpyruvate pH 7.0, 60°C Thermococcus kodakarensis
4.1.1.32 0.131
-
 phosphoenolpyruvate 60°C, pH 7.0 Thermococcus kodakarensis
4.1.1.32 0.465
-
 ATP pH 7.0, 60°C Thermococcus kodakarensis
4.1.1.32 2.23
-
 ADP pH 7.0, 60°C Thermococcus kodakarensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.32 Co2+ 21% of the activity with Mn2+ Thermococcus kodakarensis
4.1.1.32 Co2+ in the presence of one divalent cation alone, Mn2+ gives the highest activity. Mg2+ and Co2+also support the reaction, although the activities are 4.5% and 21%, respectively, of that with Mn2+. Km for Co2+: 0.752 mM. When Mg2+ is added as a second cation, in presemce of Mg2+, the Km values for CO2+ in both directions of the reaction are markedly decreased Thermococcus kodakarensis
4.1.1.32 Mg2+ 4.5% of the activity with Mn2+ Thermococcus kodakarensis
4.1.1.32 Mg2+ in the presence of one divalent cation alone, Mn2+ gives the highest activity. Mg2+ and Co2+also support the reaction, although the activities are 4.5% and 21%, respectively, of that with Mn2+. Km for Mg2+: 5.36 mM. When Mg2+ is added as a second cation, the Km values for Mn2+ in both directions of the reaction are markedly decreased to 0.021-0.022 mM Thermococcus kodakarensis
4.1.1.32 Mn2+ divalent cation required for reaction, highest activity with Mn2+ Thermococcus kodakarensis
4.1.1.32 Mn2+ in the presence of one divalent cation alone, Mn2+ gives the highest activity. Km for Mn2+: 0.263 mM. Mg2+ and Co2+also support the reaction, although the activities are 4.5% and 21%, respectively, of that with Mn2+ Thermococcus kodakarensis
4.1.1.32 additional information no activity with Ca2+, Zn2+, Cu2+, Ni2+, and Sr2+ Thermococcus kodakarensis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.32 70000
-
 4 * 70000, SDS-PAGE Thermococcus kodakarensis
4.1.1.32 72036
-
 4 * 72036, subunit mass calculated from the deduced amino acid sequence Thermococcus kodakarensis
4.1.1.32 72039
-
 4 * 72039, calculated from sequence Thermococcus kodakarensis
4.1.1.32 284000
-
 gel filtration Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.32 GTP + oxaloacetate Thermococcus kodakarensis first committed step of gluconeogenesis, important enzyme in the interconversion between C3 and C4 metabolites, recycling of an excess of phosphoenolpyruvate produced from pyruvate GDP + phosphoenolpyruvate + CO2
-
 r
4.1.1.32 GTP + oxaloacetate Thermococcus kodakarensis one of the important enzymes in the interconversion between C3 and C4 metabolites. It provides phosphoenolpyruvate from oxaloacetate as the first step of gluconeogenesis. The enzyme plays an additional role in the recycling of excess phosphoenolpyruvate produced from pyruvate, replacing the function of the anaplerotic phosphoenolpyruvate carboxylase that is missing from this archaeon GDP + phosphoenolpyruvate + CO2
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.32 Thermococcus kodakarensis Q6F494
-
-
4.1.1.32 Thermococcus kodakarensis Q6F494 hyperthermophilic archaeon, highest enzyme level when grown with pyruvate as substrate
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.32
-
 Thermococcus kodakarensis
4.1.1.32 recombinant protein Thermococcus kodakarensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.32 ATP + oxaloacetate poor substrate Thermococcus kodakarensis ADP + phosphoenolpyruvate + CO2
-
 r
4.1.1.32 ATP + oxaloacetate poor activity Thermococcus kodakarensis ADP + phosphoenolpyruvate + CO2
-
 r
4.1.1.32 GTP + oxaloacetate
-
 Thermococcus kodakarensis GDP + phosphoenolpyruvate + CO2
-
 r
4.1.1.32 GTP + oxaloacetate first committed step of gluconeogenesis, important enzyme in the interconversion between C3 and C4 metabolites, recycling of an excess of phosphoenolpyruvate produced from pyruvate Thermococcus kodakarensis GDP + phosphoenolpyruvate + CO2
-
 r
4.1.1.32 GTP + oxaloacetate one of the important enzymes in the interconversion between C3 and C4 metabolites. It provides phosphoenolpyruvate from oxaloacetate as the first step of gluconeogenesis. The enzyme plays an additional role in the recycling of excess phosphoenolpyruvate produced from pyruvate, replacing the function of the anaplerotic phosphoenolpyruvate carboxylase that is missing from this archaeon Thermococcus kodakarensis GDP + phosphoenolpyruvate + CO2
-
 r
4.1.1.32 GTP + oxaloacetate the enzyme prefers phosphoenolpyruvate formation from oxaloacetate Thermococcus kodakarensis GDP + phosphoenolpyruvate + CO2
-
 r
4.1.1.32 ITP + oxaloacetate
-
 Thermococcus kodakarensis IDP + phosphoenolpyruvate + CO2
-
 r
4.1.1.32 ITP + oxaloacetate ITP and IDP act as alternative nucleotide cofactors with similar Vmax values and slightly higher Km values Thermococcus kodakarensis IDP + phosphoenolpyruvate + CO2
-
 r

Subunits

EC Number Subunits Comment Organism
4.1.1.32 homotetramer 4 * 70000, SDS-PAGE Thermococcus kodakarensis
4.1.1.32 homotetramer 4 * 72039, calculated from sequence Thermococcus kodakarensis
4.1.1.32 tetramer 4 * 72036, subunit mass calculated from the deduced amino acid sequence Thermococcus kodakarensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.32 80
-
-
 Thermococcus kodakarensis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.1.1.32 50 90 50°C: about 45% of maximal activity, 90°C: about 80% of maximal activity Thermococcus kodakarensis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.32 80
-
 half life: 53 min Thermococcus kodakarensis
4.1.1.32 80
-
 half-life: 53 min Thermococcus kodakarensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.32 7
-
-
 Thermococcus kodakarensis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.1.32 6 8 pH 6.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity Thermococcus kodakarensis

Expression

EC Number Organism Comment Expression
4.1.1.32 Thermococcus kodakarensis higher expression levels under gluconeogenic conditions up

General Information

EC Number General Information Comment Organism
4.1.1.32 physiological function one of the important enzymes in the interconversion between C3 and C4 metabolites. It provides phosphoenolpyruvate from oxaloacetate as the first step of gluconeogenesis. The enzyme plays an additional role in the recycling of excess phosphoenolpyruvate produced from pyruvate, replacing the function of the anaplerotic phosphoenolpyruvate carboxylase that is missing from this archaeon Thermococcus kodakarensis