Literature summary for 4.2.1.11 extracted from

Lin, T.; Kornblatt, M.J.
The binding of Na(+) to apo-enolase permits the binding of substrate (2000), Biochim. Biophys. Acta, 1476, 279-286.

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Inhibitors

Inhibitors	Comment	Organism	Structure
NaClO4	inactivation is due to dissociation of the enolase into inactive monomers, 2-phospho-D-glycerate prevents this inactivation	Oryctolagus cuniculus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	three binding sites, binding at the first two is required for activity, binding at the third site is inhibitory	Oryctolagus cuniculus

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	-	rabbit	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
muscle	-	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
beta,beta-enolase	-	Oryctolagus cuniculus
enolase	-	Oryctolagus cuniculus

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Release 2023.1 (January 2023)