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Literature summary for 4.2.1.11 extracted from

  • Brewer, J.M.; Glover, C.V.C.; Holland, M.J.; Lebioda, L.
    Significance of the enzymatic properties of yeast S39A enolase to the catalytic mechanism (1998), Biochim. Biophys. Acta, 1383, 351-355.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
S39A mutant of isoenzyme 1, relative maximal velocity of 0.01% and an activation constant for Mg2+ ca. 10fold higher, compared with the native enzyme Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
phosphonoacetohydroxamate
-
Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.032
-
2-phospho-D-glycerate in presence of 1 mM Mg2+, native enzyme Saccharomyces cerevisiae
0.131
-
2-phospho-D-glycerate in presence of 1 mM Mg2+, mutant enzyme S39A Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
mutant S39A of isoenzyme 1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phospho-D-glycerate
-
Saccharomyces cerevisiae phosphoenolpyruvate
-
?
2-phospho-D-glycerate
-
Saccharomyces cerevisiae phosphoenolpyruvate + H2O
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.018 0.019 2-phospho-D-glycerate mutant enzyme S39A, pH 7.8, 21-23°C Saccharomyces cerevisiae
230
-
2-phospho-D-glycerate native enolase, pH 7.8, 21-23°C Saccharomyces cerevisiae