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Literature summary for 2.3.3.13 extracted from
- Protein acetylation on 2-isopropylmalate synthase from Thermus thermophilus HB27 (2019), Extremophiles, 23, 377-388 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | Q72JC9 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| acetylation | the enzyme is acetylated at four lysine residues. It is acetylated non-enzymatically by acetyl-CoA and deacetylated enzymatically by TT_C0104. Acetylation mimicking mutations at Lys332 markedly decreases enzyme activity in vitro, suggesting that Lys332, which is located in subdomain II, plays a regulatory role in activity | Thermus thermophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| IPMS | - |
Thermus thermophilus |
| TT_C0849 | - |
Thermus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
assay at | Thermus thermophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Thermus thermophilus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme catalyzes the first step in leucine biosynthesis | Thermus thermophilus |
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