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Literature summary for 4.2.1.11 extracted from

  • Karbassi, F.; Quiros, V.; Pancholi, V.; Kornblatt, M.J.
    Dissociation of the octameric enolase from S. pyogenes--one interface stabilizes another (2010), PLoS ONE, 5, e8810.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Streptococcus pyogenes

Protein Variants

Protein Variants Comment Organism
F137L/E363G the dimer-dimer interface mutant destabilizes the octameric structure, the double mutant is more easily dissociated in the presence of NaClO4 than is the wild type Streptococcus pyogenes

Inhibitors

Inhibitors Comment Organism Structure
NaClO4 enolase at 19.4 mM after incubation in 0.2 M NaClO4, has 32% of its original activity and is 21% octameric. Following a 24 h dialysis against buffer, the protein is 77% octameric and has 74% of its original activity Streptococcus pyogenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
452000
-
calculated molecular mass Streptococcus pyogenes

Organism

Organism UniProt Comment Textmining
Streptococcus pyogenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Streptococcus pyogenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phospho-D-glycerate
-
Streptococcus pyogenes phosphoenolpyruvate + H2O
-
r

Subunits

Subunits Comment Organism
octamer sedimentation velocity analysis Streptococcus pyogenes

Synonyms

Synonyms Comment Organism
enolase
-
Streptococcus pyogenes

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
60
-
mutant enzyme F137L/E363G, in 50 mM HEPES, pH 7.5, 1 mM Mg(OAc)2 Streptococcus pyogenes NaClO4
200
-
wild type enzyme, in 50 mM HEPES, pH 7.5, 1 mM Mg(OAc)2 Streptococcus pyogenes NaClO4