General Stability | Organism |
---|---|
limited proteolysis with trypsin results in cleavage of malate synthase into two framents of respectively 45000 Da and 19000 Da | Zea mays |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
fluoroacetate | - |
Zea mays | |
glycolate | - |
Zea mays | |
pyruvate | - |
Zea mays |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.02 | - |
acetyl-CoA | - |
Zea mays | |
0.104 | - |
glyoxylate | - |
Zea mays |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Zea mays |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA | compulsory-order mechanism, glyoxylate being the first-binding substrate, glyoxylate triggers a conformational change in the enzyme and as a consequence, the correctly shaped binding site for acetyl-CoA is created | Zea mays |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glyoxylate + acetyl-CoA + H2O | - |
Zea mays | (S)-malate + CoA | - |
? |