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Literature summary extracted from

  • Hensel, R.; Mayr, U.; Stetter, K.O.; Kandler, O.
    Comparative studies of lactic acid dehydrogenases in lactic acid bacteria. I. Purification and kinetics of the allosteric L-lactic acid dehydrogenase from Lactobacillus casei ssp. casei and Lactobacillus curvatus (1977), Arch. Microbiol., 112, 81-93.
    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 Lacticaseibacillus casei
1.1.1.27 fructose 1,6-diphosphate L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate Latilactobacillus curvatus

General Stability

EC Number General Stability Organism
1.1.1.27 irreversible loss of activity after several hours when the concentration is below 0.1 mg protein per ml Latilactobacillus curvatus
1.1.1.27 Mn2+ and fructose 1,6-diphosphate are required during dialysis at pH 5.5, very unstable during dialysis at pH 7.5 although Mn2+ and fructose 1,6-diphosphate are added Latilactobacillus curvatus
1.1.1.27 stable to dilution in the range 0.2-0.01 mg protein per ml Lacticaseibacillus casei
1.1.1.27 very stable during 70 h dialysis in acetate buffer pH 5.5, in imidazol buffer, pH 6.5, in phosphate buffer pH 6.5 with dithioerythritol and in Tris-HCl buffer pH 7.5 with Mn2+ and fructose 1,6-diphosphate Lacticaseibacillus casei

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.27 Mn2+ at low pH-values Lacticaseibacillus casei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.27 additional information
-
 additional information influence of pH Lacticaseibacillus casei
1.1.1.27 additional information
-
 additional information influence of pH Latilactobacillus curvatus
1.1.1.27 280
-
 (S)-lactate
-
 Latilactobacillus curvatus
1.1.1.27 420
-
 (S)-lactate
-
 Lacticaseibacillus casei

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.27 Ca2+ stimulation is as effective as with Mn2+, Co2+ and Cd2+ Lacticaseibacillus casei
1.1.1.27 Ca2+ 50% of the stimulation with Mn2+, Co2+ or Cd2+, higher concentrations required Latilactobacillus curvatus
1.1.1.27 Cd2+ stimulation Lacticaseibacillus casei
1.1.1.27 Cd2+ stimulation Latilactobacillus curvatus
1.1.1.27 Co2+ stimulation Lacticaseibacillus casei
1.1.1.27 Co2+ stimulation Latilactobacillus curvatus
1.1.1.27 Mn2+ stimulation Lacticaseibacillus casei
1.1.1.27 Mn2+ stimulation Latilactobacillus curvatus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Lacticaseibacillus casei
-
 ssp. casein
-
1.1.1.27 Latilactobacillus curvatus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.27
-
 Lacticaseibacillus casei
1.1.1.27
-
 Latilactobacillus curvatus

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 2030
-
-
 Latilactobacillus curvatus
1.1.1.27 2320
-
-
 Lacticaseibacillus casei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.27 (S)-lactate + NAD+ the maximal velocity of lactate oxidation is about 10% of pyruvate reduction Lacticaseibacillus casei pyruvate + NADH + H+
-
 r
1.1.1.27 (S)-lactate + NAD+ the maximal velocity of lactate oxidation is about 10% of pyruvate reduction Latilactobacillus curvatus pyruvate + NADH + H+
-
 r
1.1.1.27 pyruvate + NADH + H+ the maximal velocity of lactate oxidation is only 10% of pyruvate reduction Lacticaseibacillus casei (S)-lactate + NAD+
-
 r
1.1.1.27 pyruvate + NADH + H+ the maximal velocity of lactate oxidation is only 10% of pyruvate reduction Latilactobacillus curvatus (S)-lactate + NAD+
-
 r
1.1.1.27 pyruvate + NADPH + H+ 20% of the activity with NADH Latilactobacillus curvatus (S)-lactate + NADP+
-
 ?
1.1.1.27 pyruvate + NADPH + H+ 15% of the activity with NADH Lacticaseibacillus casei (S)-lactate + NADP+
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.27 60
-
 relatively stable Lacticaseibacillus casei
1.1.1.27 60
-
 5 min, complete inactivation without stabilizer, Mn2+ in combination with fructose 1,6-diphosphate stabilizes the enzyme completely Latilactobacillus curvatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.27 4.5
-
-
 Lacticaseibacillus casei
1.1.1.27 4.5
-
-
 Latilactobacillus curvatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 NAD+ coenzyme Lacticaseibacillus casei
1.1.1.27 NAD+ coenzyme Latilactobacillus curvatus
1.1.1.27 NADH coenzyme Lacticaseibacillus casei
1.1.1.27 NADH coenzyme Latilactobacillus curvatus
1.1.1.27 NADPH coenzyme Lacticaseibacillus casei
1.1.1.27 NADPH coenzyme Latilactobacillus curvatus