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Literature summary for 4.2.1.11 extracted from

  • Pal-Bhowmick, I.; Krishnan, S.; Jarori, G.K.
    Differential susceptibility of Plasmodium falciparum versus yeast and mammalian enolases to dissociation into active monomers (2007), FEBS J., 274, 1932-1945.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli, His-tagged recombinant protein Plasmodium falciparum

Protein Variants

Protein Variants Comment Organism
E414L replacement of an interface glutamate residue with a leucine does not result into dimer dissociation Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
KBr monomeric form Plasmodium falciparum
KCl monomeric form Plasmodium falciparum
NaCl inhibits dimeric and monomeric forms of the enzyme, inhibition stronger for the monomeric form Plasmodium falciparum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information disruption of subunit-subunit interactions declines enzyme activity 3fold Plasmodium falciparum
0.07
-
phosphoenolpyruvate acitivity for monomers Plasmodium falciparum
0.28
-
phosphoenolpyruvate activity for dimeric form Plasmodium falciparum

Metals/Ions

Metals/Ions Comment Organism Structure
KBr dimeric form 10-20% activated, monomeric form strongly inhibited Plasmodium falciparum
KCl dimeric form 10-20% activated, monomeric form strongly inhibited Plasmodium falciparum
Mg2+ protects enolases of yeast and of rabbit muscle but not of Plasmodium falciparum from dissociation in presence of imidazol Plasmodium falciparum

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum Q27727
-
-

Purification (Commentary)

Purification (Comment) Organism
gel-filtration Plasmodium falciparum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
kinetic properties of monomeric and dimeric forms of recombinant enolase compared, enzyme activity measured spectrophotometrically by monitoring formation of 2-phospho-D-glycerate, dimeric structure not essential for catalysis, monomeric form indicates a 3fold lower activity Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phospho-D-glycerate
-
Plasmodium falciparum phosphoenolpyruvate + H2O
-
r
2-phospho-D-glycerate kinetic and structural properties of monomeric and dimeric forms of recombinant enolase of Plasmodium falciparum compared Plasmodium falciparum phosphoenolpyruvate + H2O
-
r

Subunits

Subunits Comment Organism
More dissociation studies of homodimeric enolases into their active monomeric forms, analysis of intersubunit interactions and influence on catalytic and structural stability, properties of monomeric enolase determined Plasmodium falciparum

Synonyms

Synonyms Comment Organism
enolase
-
Plasmodium falciparum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
thermal stability different in monomeric and dimeric forms, the dimeric form is stable at 37°C and shows 20-25% inactivation at 50°C, the monomeric form is to 80% inactivated at 37°C after 2h and completely inactivated at 50°C Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
pH-induced dissociation of enolases, half-dissociation point Plasmodium falciparum

pH Range

pH Minimum pH Maximum Comment Organism
5 5.5 pH-dependent dissociation reveals that protonation of groups at the intersubunit interface is responsible for dissociation Plasmodium falciparum