Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CoA | two distinct CoA sites on each enzyme subunit: the first site interacts with CoA an desulfo-CoA, the second site is absolutely specific for CoA. Binding of CoA to this site occurs only when Zn2+ is present, is independent of the specific activity of the enzyme and does not eliminate CoA binding at the product site; Zn2+-dependent reversible inactivation | Saccharomyces cerevisiae | |
desulfo-CoA | - |
Saccharomyces cerevisiae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
65000 | - |
x * 65000, equilibrium sedimentation under denaturing conditions | Saccharomyces cerevisiae |
67000 | - |
2 * 67000, SDS-PAGE | Saccharomyces cerevisiae |
127000 | - |
sedimentation equilibrium centrifugation | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Saccharomyces cerevisiae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
7.1 | - |
- |
Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxo-3-methylbutanoate + acetyl-CoA + H2O | - |
Saccharomyces cerevisiae | 3-hydroxy-4-methyl-3-carboxypentanoate + CoA | i.e. alpha-isopropylmalate | ? |
Subunits | Comment | Organism |
---|---|---|
? | x * 65000, equilibrium sedimentation under denaturing conditions | Saccharomyces cerevisiae |
dimer | 2 * 67000, SDS-PAGE | Saccharomyces cerevisiae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.07 | - |
CoA | with respect to acetyl-CoA | Saccharomyces cerevisiae | |
0.09 | - |
desulfo-CoA | with respect to acetyl-CoA | Saccharomyces cerevisiae |