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Literature summary extracted from

  • Yu, L.P.; Xiang, S.; Lasso, G.; Gil, D.; Valle, M.; Tong, L.
    A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A (2009), Structure, 17, 823-832.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.4.14 acetyl-CoA allosteric activator of holoenzyme. Acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent Staphylococcus aureus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.4.14 in complex with acetyl-CoA. Acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent Staphylococcus aureus
6.4.1.1 in complex with coenzyme A, symmetrical tetramer with one coenzyme A molecule bound to each monomer. Presence of acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent Staphylococcus aureus

Protein Variants

EC Number Protein Variants Comment Organism
6.4.1.1 A610T more than 30fold loss in catalytic efficiency Staphylococcus aureus
6.4.1.1 K912T more than 30fold loss in catalytic efficiency Staphylococcus aureus
6.4.1.1 Q870A 2fold loss in catalytic efficiency Staphylococcus aureus
6.4.1.1 R644A more than 30fold loss in catalytic efficiency Staphylococcus aureus
6.4.1.1 R644K more than 30fold loss in catalytic efficiency Staphylococcus aureus
6.4.1.1 S911A 1.5fold loss in catalytic efficiency Staphylococcus aureus
6.4.1.1 T908A more than 30fold loss in catalytic efficiency Staphylococcus aureus
6.4.1.1 Y651A more than 30fold loss in catalytic efficiency Staphylococcus aureus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.4.1.1 0.58
-
 pyruvate wild-type, pH 7.5, presence of acetyl-CoA Staphylococcus aureus
6.4.1.1 1.8
-
 pyruvate mutant Q870A, pH 7.5 Staphylococcus aureus
6.4.1.1 2.3
-
 pyruvate mutant S911A, pH 7.5 Staphylococcus aureus
6.4.1.1 4.4
-
 pyruvate wild-type, pH 7.5 Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.14 Staphylococcus aureus A0A0H3JUV1 component of pyruvate carboxylase
-
6.4.1.1 Staphylococcus aureus A0A0H3JRU9
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.4.1.1 ATP + pyruvate + HCO3-
-
 Staphylococcus aureus ADP + oxaloacetate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.4.14 biotin carboxylase component of pyruvate carboxylase Staphylococcus aureus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.4.1.1 1.2
-
 pyruvate mutant Q870A, pH 7.5 Staphylococcus aureus
6.4.1.1 2.5
-
 pyruvate mutant S911A, pH 7.5 Staphylococcus aureus
6.4.1.1 6.5
-
 pyruvate wild-type, pH 7.5 Staphylococcus aureus
6.4.1.1 15.7
-
 pyruvate wild-type, pH 7.5, presence of acetyl-CoA Staphylococcus aureus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.4.1.1 0.7
-
 pyruvate mutant Q870A, pH 7.5 Staphylococcus aureus
6.4.1.1 1.1
-
 pyruvate mutant S911A, pH 7.5 Staphylococcus aureus
6.4.1.1 1.5
-
 pyruvate wild-type, pH 7.5 Staphylococcus aureus
6.4.1.1 27.2
-
 pyruvate wild-type, pH 7.5, presence of acetyl-CoA Staphylococcus aureus