Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-phospho-D-glycerate | Saccharomyces cerevisiae | - |
phosphoenolpyruvate + H2O | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P00924 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
binding affinity between enolase and phosphoglycerate mutase confirmed by interaction energies and conformation changes, 10 A resolution and three orientations positioning enolase towards to phosphoglycerate mutase tested in presence of 150 mM NaCl | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-phospho-D-glycerate | - |
Saccharomyces cerevisiae | phosphoenolpyruvate + H2O | - |
r | |
2-phospho-D-glycerate | direct transfer mechanisms of substrates between enolase and phosphoglycerate mutase predicted by molecular dynamics simulation | Saccharomyces cerevisiae | phosphoenolpyruvate + H2O | - |
r |
Synonyms | Comment | Organism |
---|---|---|
enolase | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | complex formation between active centers of enolase and phosphoglycerate mutase determined, interaction of enolase with C-terminal tail of phosphoglycerate mutase confirmed | Saccharomyces cerevisiae |