BRENDA - Enzyme Database

Reverse protonation is the key to general acid-base catalysis in enolase

Sims, P.A.; Larsen, T.M.; Poyner, R.R.; Cleland, W.W.; Reed, G.H.; Biochemistry 42, 8298-8306 (2003)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
4.2.1.11
expression of the mutants E211Q and E168Q in Escherichia coli
Saccharomyces cerevisiae
Crystallization (Commentary)
EC Number
Crystallization
Organism
4.2.1.11
mutant E211Q complexed with Mg2+ and phosphoenolpyruvate, mutant E168Q complexed with Mg2+ and 2-phospho-D-glycerate
Saccharomyces cerevisiae
Engineering
EC Number
Amino acid exchange
Commentary
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
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.11
Saccharomyces cerevisiae
P00924
-
-
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
-
650225
Saccharomyces cerevisiae
phosphoenolpyruvate
-
650225
Saccharomyces cerevisiae
r
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
4.2.1.11
expression of the mutants E211Q and E168Q in Escherichia coli
Saccharomyces cerevisiae
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.2.1.11
mutant E211Q complexed with Mg2+ and phosphoenolpyruvate, mutant E168Q complexed with Mg2+ and 2-phospho-D-glycerate
Saccharomyces cerevisiae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
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
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
-
650225
Saccharomyces cerevisiae
phosphoenolpyruvate
-
650225
Saccharomyces cerevisiae
r