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.
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 |