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Literature summary for 4.1.1.32 extracted from

  • Hlavaty, J.J.; Nowak, T.
    Characterization of the second metal site on avian phosphoenolpyruvate carboxykinase (2000), Biochemistry, 39, 1373-1388.
    View publication on PubMed
Search for more literature for 4.1.1.32

Inhibitors

Inhibitors Comment Organism Structure
Co3+-GDP competitive inhibitor Gallus gallus
Co3+-GTP competitive inhibitor Gallus gallus
Cr3+-GDP competitive inhibitor Gallus gallus
Cr3+-GTP competitive inhibitor Gallus gallus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic data for Mn2+ binding Gallus gallus
0.111
-
 oxaloacetate 25°C, apoenzyme Gallus gallus
0.123
-
 oxaloacetate 25°C, Co3+(n1)-PEPCK Gallus gallus
0.131
-
 oxaloacetate 25°C, Co3+(n1)-PEPCK-Co3+(n2)-GTP Gallus gallus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion mitochondrial isoenzyme Gallus gallus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ poor activating cation Gallus gallus
Co3+ study of Co3+-PEPCK with Co3+ bound to enzyme at site n1 Gallus gallus
Cr3+ study of Co3+-PEPCK with Cr3+ bound to enzyme at site n1 Gallus gallus
Mn2+ best activator, enzyme requires two divalent cations, one activates through a direct interaction with enzyme at site n1, located at Asp-295 and Asp-296, the second cation, at site n2, acts in the cation-nucleotide complex that serves as a substrate, role and binding mode of Mn2+, may be a regulator for enzyme in vivo Gallus gallus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
67000
-
 1 * 67000 Gallus gallus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + oxaloacetate Gallus gallus committed step in gluconeogenesis GDP + phosphoenolpyruvate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Oxidation Stability

Oxidation Stability Organism
PEPCK is very stable toward oxidative treatment Gallus gallus

Purification (Commentary)

Purification (Comment) Organism
-
 Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Gallus gallus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Gallus gallus

Storage Stability

Storage Stability Organism
4°C, Co3+-PEPCK with Co3+ bound to enzyme at site n1, 1 week, stable Gallus gallus
4°C, Cr3+-PEPCK with Cr3+ bound to enzyme at site n1, at least 3 days, stable Gallus gallus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + oxaloacetate metal-nucleotide complex serves as substrate, active site structure, a conformational change at the active site occurs during catalysis Gallus gallus GDP + phosphoenolpyruvate + CO2
-
 r
GTP + oxaloacetate committed step in gluconeogenesis Gallus gallus GDP + phosphoenolpyruvate + CO2
-
 ?
ITP + oxaloacetate
-
 Gallus gallus IDP + phosphoenolpyruvate + CO2
-
 r
additional information not: ATP Gallus gallus ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 67000 Gallus gallus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Gallus gallus