BRENDA - Enzyme Database

Structural flexibility in Trypanosoma brucei enolase revealed by X-ray crystallography and molecular dynamics

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.; FEBS J. 274, 5077-5089 (2007)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
4.2.1.11
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)
EC Number
Commentary
Organism
4.2.1.11
recombinant enolase, expressed in Escherichia coli BL21-DE3-pLysS strain harbouring the recombinant pET28a plasmid
Trypanosoma brucei
Crystallization (Commentary)
EC Number
Crystallization
Organism
4.2.1.11
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
EC Number
Inhibitors
Commentary
Organism
Structure
4.2.1.11
2-fluoro-2-phosphonoacetohydroxamate
competitive inhibitor
Trypanosoma brucei
4.2.1.11
phosphonoacetohydroxamate
retains open tunnel from catalytic site to protein surface, offers possibilities for drug development
Trypanosoma brucei
4.2.1.11
SO42-
induces a complete closure of catalytic site loops
Trypanosoma brucei
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.11
Mg2+
activity depends on
Trypanosoma brucei
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.11
2-phospho-D-glycerate
Trypanosoma brucei
-
phosphoenolpyruvate + H2O
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.11
Trypanosoma brucei
Q9NDH8
-
-
Purification (Commentary)
EC Number
Commentary
Organism
4.2.1.11
recombinant protein
Trypanosoma brucei
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.2.1.11
additional information
-
activity assay of recombinant protein
Trypanosoma brucei
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
-
679787
Trypanosoma brucei
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
structural analysis
679787
Trypanosoma brucei
phosphoenolpyruvate + H2O
-
-
-
r
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
4.2.1.11
25
-
activity assay at
Trypanosoma brucei
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.2.1.11
7.5
-
activity assay at
Trypanosoma brucei
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.2.1.11
0.0014
-
2-fluoro-2-phosphonoacetohydroxamate
at pH 7.2, binds in the same way as phosphoenolpyruvate and phosphonoacetohydroxamate
Trypanosoma brucei
4.2.1.11
0.015
-
phosphonoacetohydroxamate
-
Trypanosoma brucei
Application (protein specific)
EC Number
Application
Commentary
Organism
4.2.1.11
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) (protein specific)
EC Number
Commentary
Organism
4.2.1.11
recombinant enolase, expressed in Escherichia coli BL21-DE3-pLysS strain harbouring the recombinant pET28a plasmid
Trypanosoma brucei
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.2.1.11
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 (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.2.1.11
2-fluoro-2-phosphonoacetohydroxamate
competitive inhibitor
Trypanosoma brucei
4.2.1.11
phosphonoacetohydroxamate
retains open tunnel from catalytic site to protein surface, offers possibilities for drug development
Trypanosoma brucei
4.2.1.11
SO42-
induces a complete closure of catalytic site loops
Trypanosoma brucei
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.2.1.11
0.0014
-
2-fluoro-2-phosphonoacetohydroxamate
at pH 7.2, binds in the same way as phosphoenolpyruvate and phosphonoacetohydroxamate
Trypanosoma brucei
4.2.1.11
0.015
-
phosphonoacetohydroxamate
-
Trypanosoma brucei
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.11
Mg2+
activity depends on
Trypanosoma brucei
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.11
2-phospho-D-glycerate
Trypanosoma brucei
-
phosphoenolpyruvate + H2O
-
-
r
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.2.1.11
recombinant protein
Trypanosoma brucei
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.2.1.11
additional information
-
activity assay of recombinant protein
Trypanosoma brucei
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
-
679787
Trypanosoma brucei
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
structural analysis
679787
Trypanosoma brucei
phosphoenolpyruvate + H2O
-
-
-
r
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
4.2.1.11
25
-
activity assay at
Trypanosoma brucei
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.2.1.11
7.5
-
activity assay at
Trypanosoma brucei