Literature summary for 4.2.1.11 extracted from

de A. S. Navarro, M.V.; Gomes Dias, S.M.; Mello, L.V.; da Silva Giotto, M.T.; Gavalda, S.; Blonski, C.; Garratt, R.C.; Rigden, D.J.
Structural flexibility in Trypanosoma brucei enolase revealed by X-ray crystallography and molecular dynamics (2007), FEBS J., 274, 5077-5089.

Search for more literature for 4.2.1.11

Application

Application	Comment	Organism
drug development	structure and molecular dynamics applied to design irreversible species-specific inhibitors, parasite-specific lysine residue closely to catalytic site identified	Trypanosoma brucei

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant enolase, expressed in Escherichia coli BL21-DE3-pLysS strain harbouring the recombinant pET28a plasmid	Trypanosoma brucei

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop method, six novel crystal structures with various ligation states and conformations identified, high structural diversity of loops near the catalytic site determined, novel metal-binding site within the catalytic site identified	Trypanosoma brucei

Inhibitors

Inhibitors	Comment	Organism	Structure
2-fluoro-2-phosphonoacetohydroxamate	competitive inhibitor	Trypanosoma brucei
phosphonoacetohydroxamate	retains open tunnel from catalytic site to protein surface, offers possibilities for drug development	Trypanosoma brucei
SO42-	induces a complete closure of catalytic site loops	Trypanosoma brucei

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	activity depends on	Trypanosoma brucei

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2-phospho-D-glycerate	Trypanosoma brucei	-	phosphoenolpyruvate + H2O	-	r

Organism

Organism	UniProt	Comment	Textmining
Trypanosoma brucei	Q9NDH8	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant protein	Trypanosoma brucei

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	activity assay of recombinant protein	Trypanosoma brucei

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-phospho-D-glycerate	-	Trypanosoma brucei	phosphoenolpyruvate + H2O	-	r
2-phospho-D-glycerate	structural analysis	Trypanosoma brucei	phosphoenolpyruvate + H2O	-	r

Synonyms

Synonyms	Comment	Organism
enolase	-	Trypanosoma brucei

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	activity assay at	Trypanosoma brucei

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	activity assay at	Trypanosoma brucei

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.0014	-	2-fluoro-2-phosphonoacetohydroxamate	at pH 7.2, binds in the same way as phosphoenolpyruvate and phosphonoacetohydroxamate	Trypanosoma brucei
0.015	-	phosphonoacetohydroxamate	-	Trypanosoma brucei

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Release 2023.1 (January 2023)