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Literature summary extracted from

  • Mou, L.; Mulvena, D.P.; Jonas, H.A.; Jago, G.R.
    Purification and properties of nicotinamide adenine dinucleotide-dependent D- and L-lactate dehydrogenases in a group N streptococcus (1972), J. Bacteriol., 111, 392-396.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Lactococcus lactis
-
-
-
1.1.1.27 Lactococcus lactis 760
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.27
-
 Lactococcus lactis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.27 additional information
-
-
 Lactococcus lactis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.27 (S)-lactate + NAD+
-
 Lactococcus lactis pyruvate + NADH + H+
-
 r
1.1.1.27 (S)-lactate + NAD+
-
 Lactococcus lactis 760 pyruvate + NADH + H+
-
 r
1.1.1.27 pyruvate + NADH + H+
-
 Lactococcus lactis (S)-lactate + NAD+
-
 r
1.1.1.27 pyruvate + NADH + H+
-
 Lactococcus lactis 760 (S)-lactate + NAD+
-
 r

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.27 5 7 reduction of pyruvate, in presence of fructose 1,6-diphosphate Lactococcus lactis
1.1.1.27 8
-
 reduction of pyruvate, in absence of fructose 1,6-diphosphate Lactococcus lactis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.27 5 7.5 rapid loss of activity below pH 5.0 and above pH 7.5 Lactococcus lactis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 NAD+ coenzyme Lactococcus lactis
1.1.1.27 NADH coenzyme Lactococcus lactis