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Literature summary for 2.3.3.9 extracted from
- Molecular structure of malate synthase and structural change upon ligand binding to the enzyme (1974), Biochem. Biophys. Res. Commun., 58, 419-426.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | causes no structurel effects, suggesting the metal ion to be involved in enzymatic catalysis rather than structural alternations | Saccharomyces cerevisiae |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 70000 | - |
4 * 70000, SDS-PAGE | Saccharomyces cerevisiae |
| 170000 | - |
gel filtration, ultracentrifugation, sucrose density gradient centrifugation | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glyoxylate + acetyl-CoA + H2O | - |
Saccharomyces cerevisiae | (S)-malate + CoA | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | 4 * 70000, SDS-PAGE | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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