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Literature summary for 4.2.1.11 extracted from

  • Poyner, R.R.; Laughlin, L.T.; Sowa, G.A.; Reed, G.H.
    Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants (1996), Biochemistry, 35, 1692-1699.
    View publication on PubMed
Search for more literature for 4.2.1.11

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant genes in Escherichia coli Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E168Q severely depressed activity, does not catalyze hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3, alters the tautomeric state or catalyzes ionization of bound tartronate semialdehyde phosphate Saccharomyces cerevisiae
E211Q severely depressed activity, alters the tautomeric state or catalyzes ionization of bound tartronate semialdehyde phosphate. Glu211 participates in the second step of the reaction Saccharomyces cerevisiae
K345A severely depressed activity, does not catalyze hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3, fails to catalyze the exchange of the C-2 proton of 2-phospho-D-glycerate with deuterium in D2O, inactive in ionization of tartronate semialdehyde phosphate. Lys345 functions as the base in the ionization of 2-phosphoglycerate Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.11
-
 2-phospho-D-glycerate mutant E168Q Saccharomyces cerevisiae
0.12
-
 2-phospho-D-glycerate mutant enzyme E211Q Saccharomyces cerevisiae
0.3
-
 2-phospho-D-glycerate wild type enzyme Saccharomyces cerevisiae
0.68
-
 2-phospho-D-glycerate mutant K345A Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(Z)-3-chloro-2-phosphoenolpyruvate + OH- wild-type enzyme catalyzes hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3 Saccharomyces cerevisiae ?
-
 ?
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
78
-
 2-phospho-D-glycerate wild-type enzyme Saccharomyces cerevisiae