Activating Compound | Comment | Organism | Structure |
---|---|---|---|
D-fructose 1,6-bisphosphate | activation constants of isozymes at different pH values, overview | Lactococcus lactis |
Cloned (Comment) | Organism |
---|---|
genes ldh and ldhB, sequence determination, analysis, and comparison | Lactococcus lactis |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of an ldh gene insertion mutant strain FI9078, the insertion of an IS905-like element, that created a hybrid promoter in the intergenic region upstream of ldhB, leads to activation of a second isozyme LDHB, which shows a strongly pH-dependent activity, overview | Lactococcus lactis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
phosphate | phosphate acts as a strong activator of LDHB | Lactococcus lactis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | isozymes LDH and LDHB, kinetic analysis, NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH does not change with pH | Lactococcus lactis | |
0.054 | - |
NADH | pH 6.0, 30°C, isozyme LDH | Lactococcus lactis | |
0.058 | - |
NADH | pH 7.0, 30°C, isozyme LDH | Lactococcus lactis | |
0.077 | - |
NADH | pH 6.0, 30°C, isozyme LDHB | Lactococcus lactis | |
0.364 | - |
NADH | pH 7.0, 30°C, isozyme LDHB | Lactococcus lactis | |
1.3 | - |
pyruvate | pH 6.0, 30°C, isozyme LDHB | Lactococcus lactis | |
1.5 | - |
pyruvate | pH 6.0, 30°C, isozyme LDH | Lactococcus lactis | |
1.7 | - |
pyruvate | pH 7.0, 30°C, isozyme LDH | Lactococcus lactis | |
2.9 | - |
pyruvate | pH 7.0, 30°C, isozyme LDHB | Lactococcus lactis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + NAD+ | Lactococcus lactis | LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis | pyruvate + NADH + H+ | - |
r | |
(S)-lactate + NAD+ | Lactococcus lactis MG1363 | LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis | pyruvate + NADH + H+ | - |
r | |
additional information | Lactococcus lactis | intracellular isozyme regulation in relation to pH, overview | ? | - |
? | |
additional information | Lactococcus lactis MG1363 | intracellular isozyme regulation in relation to pH, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lactococcus lactis | P0C2T6 | genes ldh and ldhB | - |
Lactococcus lactis MG1363 | P0C2T6 | genes ldh and ldhB | - |
Purification (Comment) | Organism |
---|---|
isozymes LDHB and LDH 400fold and 30fold, from cell extracts of strains FI9078 and MG1363, respectively | Lactococcus lactis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + NAD+ | LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis | Lactococcus lactis | pyruvate + NADH + H+ | - |
r | |
(S)-lactate + NAD+ | LDH posseses a catalytic His171 residue | Lactococcus lactis | pyruvate + NADH + H+ | - |
r | |
(S)-lactate + NAD+ | LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis | Lactococcus lactis MG1363 | pyruvate + NADH + H+ | - |
r | |
(S)-lactate + NAD+ | LDH posseses a catalytic His171 residue | Lactococcus lactis MG1363 | pyruvate + NADH + H+ | - |
r | |
additional information | intracellular isozyme regulation in relation to pH, overview | Lactococcus lactis | ? | - |
? | |
additional information | intracellular isozyme regulation in relation to pH, overview | Lactococcus lactis MG1363 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | LDH has a slightly larger negative charge than LDHB and a greater concentration of positive charges at the interface between monomers | Lactococcus lactis |
Synonyms | Comment | Organism |
---|---|---|
LDH | - |
Lactococcus lactis |
LDHB | - |
Lactococcus lactis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Lactococcus lactis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | 6 | isozyme LDHB | Lactococcus lactis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
the two isozymes LDH and LDHB exhibited different pH profiles for maximal activity | Lactococcus lactis |
5.2 | 7.2 | LDH activity shows a broad plateau between pH 5.2 and pH 7.2, and no activity at pH 4.8 | Lactococcus lactis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Lactococcus lactis | |
NADH | NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH did not change with pH | Lactococcus lactis |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Lactococcus lactis | isozyme LDH, sequence calculation | - |
4.9 |
Lactococcus lactis | isozyme LDHB, sequence calculation | - |
5.2 |