Protein Variants | Comment | Organism |
---|---|---|
E155A | mutant enzyme exhibits 1000fold lower activity than wild-type enzyme. Activity of E155A can be partially rescued by formate | Saccharomyces cerevisiae |
E155Q | mutant enzyme exhibits 1000fold lower activity than wild-type enzyme. The kcat for E155Q decreases at high pH, similar to the wild-type enzyme, but is pH independent at low pH | Saccharomyces cerevisiae |
H309A | inactive mutant enzyme. Slight increase in activity is observed for H309A in the presence of 300 mM imidazole, which is still 1000fold lower than that of wild type | Saccharomyces cerevisiae |
H309N | inactive mutant enzyme | Saccharomyces cerevisiae |
Y320F | mutant enzyme loses 25fold activity compared to that of the wild-type enzyme | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.039 | - |
acetyl-CoA | mutant enzyme E155A | Saccharomyces cerevisiae | |
0.14 | - |
acetyl-CoA | wild-type enzyme | Saccharomyces cerevisiae | |
0.14 | - |
acetyl-CoA | mutant enzyme Y320F | Saccharomyces cerevisiae | |
13 | - |
2-oxoglutarate | mutant enzyme E155A | Saccharomyces cerevisiae | |
33 | - |
2-oxoglutarate | mutant enzyme Y320F | Saccharomyces cerevisiae | |
42 | - |
2-oxoglutarate | wild-type enzyme | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + H2O + 2-oxoglutarate | a catalytic dyad comprising Glu155 and His309 acts to deprotonate the methyl group of acetyl-CoA, while Tyr320 is likely not directly involved in catalysis, but may aid in orienting the reactant and/or the catalytic dyad | Saccharomyces cerevisiae | 2-hydroxybutane-1,2,4-tricarboxylate + CoA | - |
? |
Synonyms | Comment | Organism |
---|---|---|
acetyl-coenzyme A: 2-ketoglutarate C-transferase | - |
Saccharomyces cerevisiae |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | the kcat for E155Q decreases at high pH, similar to the wild type enzyme, but is pH independent at low pH | Saccharomyces cerevisiae |