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Literature summary for 6.4.1.1 extracted from

  • Adina-Zada, A.; Hazra, R.; Sereeruk, C.; Jitrapakdee, S.; Zeczycki, T.; Maurice, M.; Cleland, W.; Wallace, J.; Attwood, P.
    Probing the allosteric activation of pyruvate carboxylase using 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate as a fluorescent mimic of the allosteric activator acetyl CoA (2011), Arch. Biochem. Biophys., 509, 117-126.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate allosteric activator of pyruvate carboxylase. The increase in activity between 2 mM and saturating MgATP is approximately 16fold Rhizobium etli
acetyl-CoA allosteric activator of pyruvate carboxylase, there is a 7fold increase in the turnover number for ATP cleavage induced by acetyl-CoA Rhizobium etli

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Rhizobium etli

Protein Variants

Protein Variants Comment Organism
R472S the mutation severely decreases the affinity of the enzyme for acetyl-CoA Rhizobium etli

Inhibitors

Inhibitors Comment Organism Structure
2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate inhibitor with respect to MgATP2- Rhizobium etli
ATP at concentrations above saturating, MgATP2- activates bicarbonate-dependent ATP cleavage, but inhibits the overall reaction Rhizobium etli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Rhizobium etli

Organism

Organism UniProt Comment Textmining
Rhizobium etli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Co2+-affinity column chromatography Rhizobium etli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pyruvate + HCO3- + H+
-
Rhizobium etli ADP + oxaloacetate + phosphate
-
?
additional information 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate is no substrate Rhizobium etli ?
-
?

Cofactor

Cofactor Comment Organism Structure
ATP at concentrations above saturating, MgATP2- activates bicarbonate-dependent ATP cleavage, but inhibits the overall reaction Rhizobium etli