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 |
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 |
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 |
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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.4.14 | Staphylococcus aureus | A0A0H3JUV1 | component of pyruvate carboxylase | - |
6.4.1.1 | Staphylococcus aureus | A0A0H3JRU9 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.4.1.1 | ATP + pyruvate + HCO3- | - |
Staphylococcus aureus | ADP + oxaloacetate + phosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.3.4.14 | biotin carboxylase | component of pyruvate carboxylase | Staphylococcus aureus |
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 |
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 |