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Literature summary for 6.4.1.1 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
Search for more literature for 6.4.1.1

Protein Variants

Protein Variants Comment Organism
K119Q no catalytic acitivy for pyruvate decarboxylation, or oxaloacetate decarboxylation Rhizobium etli
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
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
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
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
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

Inhibitors Comment Organism Structure
oxamate substrate inhibition Rhizobium etli
pyruvate substrate inhibition Rhizobium etli

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Rhizobium etli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

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

Ki Value [mM]

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