Inhibitors | Comment | Organism | Structure |
---|---|---|---|
lysine | strong allosteric inhibitor of Lys21p. Induces positive cooperativity for alpha-ketoglutarate binding | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + H2O + 2-oxoglutarate | Saccharomyces cerevisiae | in the yeast Saccharomyces cerevisiae, the first committed step of the lysine biosynthetic pathway is catalysed by two homocitrate synthases encoded by LYS20 and LYS21. During growth on ethanol, homocitrate is mainly synthesized through Lys21p, while under fermentative metabolism, Lys20p and Lys21p play redundant roles | 2-hydroxybutane-1,2,4-tricarboxylate + CoA | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P48570 | - |
- |
Saccharomyces cerevisiae | Q12122 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + H2O + 2-oxoglutarate | in the yeast Saccharomyces cerevisiae, the first committed step of the lysine biosynthetic pathway is catalysed by two homocitrate synthases encoded by LYS20 and LYS21. During growth on ethanol, homocitrate is mainly synthesized through Lys21p, while under fermentative metabolism, Lys20p and Lys21p play redundant roles | Saccharomyces cerevisiae | 2-hydroxybutane-1,2,4-tricarboxylate + CoA | - |
? |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.053 | - |
lysine | - |
Saccharomyces cerevisiae |