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Literature summary extracted from

  • Sims, P.A.; Larsen, T.M.; Poyner, R.R.; Cleland, W.W.; Reed, G.H.
    Reverse protonation is the key to general acid-base catalysis in enolase (2003), Biochemistry, 42, 8298-8306.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.11 expression of the mutants E211Q and E168Q in Escherichia coli Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.11 mutant E211Q complexed with Mg2+ and phosphoenolpyruvate, mutant E168Q complexed with Mg2+ and 2-phospho-D-glycerate Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.11 E168Q the Mg2+ binding site is different compared to the wild type enzyme Saccharomyces cerevisiae
4.2.1.11 E211Q can exchange the alpha proton of 2-phospho-D-glycerate, but cannot catalyze the complete dehydration to phosphoenolpyruvate Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.11 Saccharomyces cerevisiae P00924
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.11 2-phospho-D-glycerate
-
Saccharomyces cerevisiae phosphoenolpyruvate
-
r

Synonyms

EC Number Synonyms Comment Organism
4.2.1.11 enolase
-
Saccharomyces cerevisiae