Cloned (Comment) | Organism |
---|---|
catalytic domain, residues 173-427 | Geobacillus stearothermophilus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.013 | - |
acetyl-CoA | catalytic domain after expression in Escherichia coli | Geobacillus stearothermophilus | |
1.2 | - |
dihydrolipoamide | catalytic domain after expression in Escherichia coli | Geobacillus stearothermophilus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
additional information | - |
high molecular mass species in the absence of guanidinium hydrochloride | Geobacillus stearothermophilus |
30000 | - |
gel filtration in the presence of guanidinium hydrochloride | Geobacillus stearothermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dihydrolipoamide + acetyl-CoA | Geobacillus stearothermophilus | - |
S-acetyldihydrolipoamide + CoA | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Geobacillus stearothermophilus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Geobacillus stearothermophilus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine | reaction mechanism | Geobacillus stearothermophilus |
Renatured (Comment) | Organism |
---|---|
treatment with guanidine hydrochloride results in dissociation into subunits, removal of guanidine hydrochloride results in refolding of the enzyme with 95% of the original activity | Geobacillus stearothermophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dihydrolipoamide + acetyl-CoA | - |
Geobacillus stearothermophilus | S-acetyldihydrolipoamide + CoA | - |
? |