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Literature summary for 1.1.1.27 extracted from

  • Hardman, M.J.; Pritchard, G.G.
    Kinetics of activation of L-lactate dehydrogenase from Streptococcus faecalis by fructose 1,6-bisphosphate and by metal ions (1987), Biochim. Biophys. Acta, 912, 185-190.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
fructose 1,6-diphosphate L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate Enterococcus faecalis
fructose 1,6-diphosphate binding of fructose 1,6-diphosphate induces a conformational change in the enzyme which leads to increased activity, without association of enzyme subunits or dimers Enterococcus faecalis

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ stimulation Enterococcus faecalis
Co2+ activation involves association of enzyme dimers, followed by ligand binding Enterococcus faecalis
Mn2+ stimulation Enterococcus faecalis

Organism

Organism UniProt Comment Textmining
Enterococcus faecalis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + NADH + H+
-
Enterococcus faecalis (S)-lactate + NAD+
-
?

Cofactor

Cofactor Comment Organism Structure
NADH coenzyme Enterococcus faecalis