Literature summary for 4.2.1.11 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.

Search for more literature for 4.2.1.11

Cloned(Commentary)

Cloned (Comment)	Organism
expression of the mutants E211Q and E168Q in Escherichia coli	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant E211Q complexed with Mg2+ and phosphoenolpyruvate, mutant E168Q complexed with Mg2+ and 2-phospho-D-glycerate	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
E168Q	the Mg2+ binding site is different compared to the wild type enzyme	Saccharomyces cerevisiae
E211Q	can exchange the alpha proton of 2-phospho-D-glycerate, but cannot catalyze the complete dehydration to phosphoenolpyruvate	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P00924	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
enolase	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)