Activating Compound | Comment | Organism | Structure |
---|---|---|---|
D-fructose-1,6-bisphophate | FBP, L-nLDH activity is FBP dependent | Lactococcus cremoris |
Cloned (Comment) | Organism |
---|---|
gene ldh, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain M15 | Lactococcus cremoris |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ADP | ADP is a more severe inhibitor and has a more severe inhibitory effect on the lactate oxidation reaction. But its relative inhibition on reverse reactions is weak at low ADP concentrations | Lactococcus cremoris | |
ATP | inhibitory effects of ATP on both directions are weak and similar as both rates remain above 80% in the presence of 8 mM ATP | Lactococcus cremoris | |
Lactate | a high concentration of lactate has a weak inhibitory effect on the pyruvate reduction reaction activity but is meaningful for a significant lactate oxidation rate as the K m value of LDHA for L-lactate is very high | Lactococcus cremoris |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | enzyme kinetics, ordered bibi kinetic mechanism of nLDH with the coenzyme binding first | Lactococcus cremoris | |
0.066 | - |
NADH | pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate | Lactococcus cremoris | |
0.38 | - |
NAD+ | pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate | Lactococcus cremoris | |
1.95 | - |
pyruvate | pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate | Lactococcus cremoris | |
158 | - |
(S)-lactate | pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate | Lactococcus cremoris |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + NAD+ | Lactococcus cremoris | lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels | pyruvate + NADH + H+ | - |
r | |
(S)-lactate + NAD+ | Lactococcus cremoris MG1363 | lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels | pyruvate + NADH + H+ | - |
r | |
pyruvate + NADH + H+ | Lactococcus cremoris | - |
(S)-lactate + NAD+ | - |
r | |
pyruvate + NADH + H+ | Lactococcus cremoris MG1363 | - |
(S)-lactate + NAD+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lactococcus cremoris | - |
- |
- |
Lactococcus cremoris MG1363 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant C-terminally His-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography | Lactococcus cremoris |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(S)-lactate + NAD+ = pyruvate + NADH + H+ | the enzyme LDHA shows an ordered bibi kinetic mechanism of nLDH with the coenzyme binding first | Lactococcus cremoris |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cell culture | FBP-activated L-nLDH activity is constantly very significant throughout the growth period, even when lactate is consumed in the stationary phase of respiration. During the lactate utilization period, L-nLDH activity is regulated by some factors and the pyruvate reduction activity is completely inhibited or masked | Lactococcus cremoris | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
9.3 | 12.2 | native enzyme in strain MG1363 at different growth phases and conditions, pH 7.0, 30°C | Lactococcus cremoris |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + NAD+ | - |
Lactococcus cremoris | pyruvate + NADH + H+ | - |
r | |
(S)-lactate + NAD+ | lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels | Lactococcus cremoris | pyruvate + NADH + H+ | - |
r | |
(S)-lactate + NAD+ | - |
Lactococcus cremoris MG1363 | pyruvate + NADH + H+ | - |
r | |
(S)-lactate + NAD+ | lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels | Lactococcus cremoris MG1363 | pyruvate + NADH + H+ | - |
r | |
pyruvate + NADH + H+ | - |
Lactococcus cremoris | (S)-lactate + NAD+ | - |
r | |
pyruvate + NADH + H+ | - |
Lactococcus cremoris MG1363 | (S)-lactate + NAD+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
L-nLDH | - |
Lactococcus cremoris |
LDH | - |
Lactococcus cremoris |
LdhA | - |
Lactococcus cremoris |
NAD-dependent lactate dehydrogenase | - |
Lactococcus cremoris |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Lactococcus cremoris |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Lactococcus cremoris |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Lactococcus cremoris | |
NADH | - |
Lactococcus cremoris |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | inhibition kinetics | Lactococcus cremoris |
General Information | Comment | Organism |
---|---|---|
evolution | genes ldh, ldhB and ldhX, are transcribed to some extent in Lactococcus lactis strain MG1363. The product of the ldhX gene has little nLDH activity as well as ldhB which exhibits only leaky transcription and plays a minor role in lactate yield. LDHA encoded by ldh has been found to perform major L-nLDH activity, with the contribution of other alternate L-nLDHs being small | Lactococcus cremoris |
metabolism | NAD-dependent lactate dehydrogenase catalyses the first step in respiratory utilization of lactate by Lactococcus lactis | Lactococcus cremoris |