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Literature summary 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

EC Number Activating Compound Comment Organism Structure
1.1.1.27 fructose 1,6-diphosphate L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate Enterococcus faecalis
1.1.1.27 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

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Enterococcus faecalis
-
-
-

Substrates and Products (Substrate)

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 NADH coenzyme Enterococcus faecalis