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Literature summary for 4.2.1.11 extracted from

  • Hakobyan, D.; Nazaryan, K.
    Investigation of interaction between enolase and phosphoglycerate mutase using molecular dynamics simulation (2006), J. Biomol. Struct. Dyn., 23, 625-633.
    View publication on PubMed
Search for more literature for 4.2.1.11

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-phospho-D-glycerate Saccharomyces cerevisiae
-
 phosphoenolpyruvate + H2O
-
 r

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P00924
-
-

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
enolase
-
 Saccharomyces cerevisiae

Cofactor

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