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Literature summary extracted from

  • Zeczycki, T.N.; St Maurice, M.; Jitrapakdee, S.; Wallace, J.C.; Attwood, P.V.; Cleland, W.W.
    Insight into the carboxyl transferase domain mechanism of pyruvate carboxylase from Rhizobium etli (2009), Biochemistry, 48, 4305-4313.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
6.4.1.1 K119Q no catalytic acitivy for pyruvate decarboxylation, or oxaloacetate decarboxylation Rhizobium etli
6.4.1.1 K718Q 2.9% of wild-type activity for pyruvate carboxylation, 14% for full reverse reaction, 7.2% for oxaloacetate decarboxylation in presence of oxamate Rhizobium etli
6.4.1.1 Q844L/S885A 13% of wild-type activity for pyruvate carboxylation, 53% for full reverse reaction, 4.7% for oxaloacetate decarboxylation in presence of oxamate Rhizobium etli
6.4.1.1 T882A no catalytic activity for reactions involving the carboxyl transferase domain. 7- and 3.5fold increases in activity, as compared to that of the wild-type enzyme, for the ADP phosphorylation and bicarbonate-dependent ATPase reactions, respectively. Partial inhibition of the T882A-catalyzed biotin carboxylase domain reactions by oxamate and pyruvate Rhizobium etli
6.4.1.1 T882C 7.1% of wild-type activity for pyruvate carboxylation, 20% for full reverse reaction, 11% for oxaloacetate decarboxylation in presence of oxamate Rhizobium etli
6.4.1.1 T882S 21% of wild-type activity for pyruvate carboxylation, 51% for full reverse reaction, 30% for oxaloacetate decarboxylation in presence of oxamate Rhizobium etli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.4.1.1 oxamate substrate inhibition Rhizobium etli
6.4.1.1 pyruvate substrate inhibition Rhizobium etli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.4.1.1 1
-
 pyruvate ATPase reaction, wild-type, pH 7.5, 25°C Rhizobium etli
6.4.1.1 4.1
-
 oxamate ATPase reaction, wild-type, pH 7.5, 25°C Rhizobium etli

Organism

EC Number Organism UniProt Comment Textmining
6.4.1.1 Rhizobium etli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate catalytic mechanism involves the decarboxylation of carboxybiotin and removal of a proton from Thr882 by the resulting biotin enolate with either a concerted or subsequent transfer of a proton from pyruvate to Thr882. The resulting enolpyruvate then reacts with CO2 to form oxaloacetate and complete the reaction Rhizobium etli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.4.1.1 ATP + oxamate + HCO3- + H+
-
 Rhizobium etli ADP + phosphate + ?
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Rhizobium etli ADP + phosphate + oxaloacetate
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.4.1.1 10
-
 pyruvate ATPase reaction, wild-type, pH 7.5, 25°C Rhizobium etli
6.4.1.1 10.1
-
 oxamate ATPase reaction, wild-type, pH 7.5, 25°C Rhizobium etli