BRENDA - Enzyme Database

Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution

Zhang, E.; Brewer, J.M.; Minor, W.; Carreira, L.A.; Lebioda, L.; Biochemistry 36, 12526-12534 (1997)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
4.2.1.11
crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution
Saccharomyces cerevisiae
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.11
Saccharomyces cerevisiae
P00924
-
-
Reaction
EC Number
Reaction
Commentary
Organism
4.2.1.11
2-phospho-D-glycerate = phosphoenolpyruvate + H2O
mechanism
Saccharomyces cerevisiae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.11
2-phospho-D-glycerate
-
33643
Saccharomyces cerevisiae
phosphoenolpyruvate
-
33643
Saccharomyces cerevisiae
?
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.2.1.11
crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.11
2-phospho-D-glycerate
-
33643
Saccharomyces cerevisiae
phosphoenolpyruvate
-
33643
Saccharomyces cerevisiae
?