Inhibitors | Comment | Organism | Structure |
---|---|---|---|
pyruvate | low substrate inhibition | Faxonius virilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Vmax in the pyruvate-reducing direction is significantly higher for the enzyme from anoxic crayfish whereas in the lactate-oxidizing direction the Vmax is significantly higher for the aerobic control enzyme | Faxonius virilis | |
0.123 | - |
pyruvate | aerobic control enzyme, pH 6.7, 25°C | Faxonius virilis | |
0.19 | - |
pyruvate | anoxic enzyme, pH 6.7, 25°C | Faxonius virilis | |
0.353 | - |
pyruvate | anoxic enzyme, pH 7.2, 25°C | Faxonius virilis | |
0.36 | - |
pyruvate | aerobic control enzyme, pH 7.2, 25°C | Faxonius virilis | |
1.96 | - |
NAD+ | anoxic enzyme, pH 8.5, 25°C | Faxonius virilis | |
2.18 | - |
NAD+ | aerobic control enzyme, pH 8.5, 25°C | Faxonius virilis | |
22 | - |
(S)-lactate | anoxic enzyme, pH 6.7, 25°C | Faxonius virilis | |
32.9 | - |
(S)-lactate | aerobic control enzyme, pH 8.5, 25°C | Faxonius virilis | |
34.2 | - |
(S)-lactate | anoxic enzyme, pH 8.5, 25°C | Faxonius virilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + NAD+ | Faxonius virilis | - |
pyruvate + NADH + H+ | - |
r | |
pyruvate + NADH + H+ | Faxonius virilis | - |
(S)-lactate + NAD+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Faxonius virilis | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | purified LDH from aerobic control crayfish shows significantly higher amounts of serine/threonine phosphorylation than does the anoxic enzyme form | Faxonius virilis |
Purification (Comment) | Organism |
---|---|
native enzyme to homogeneity from tail muscle of both aerobic control and anoxic crayfish 26.5fold and 69.4fold, respectively, by anion exchange chromatography and two steps of affinity chromatography | Faxonius virilis |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
tail muscle | - |
Faxonius virilis | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
7.35 | - |
purified native aerobic control enzyme, pH 7.2, 25°C, pyruvate reduction | Faxonius virilis |
15.8 | - |
purified native anoxic enzyme, pH 7.2, 25°C, pyruvate reduction | Faxonius virilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + NAD+ | - |
Faxonius virilis | pyruvate + NADH + H+ | - |
r | |
pyruvate + NADH + H+ | - |
Faxonius virilis | (S)-lactate + NAD+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
lactate dehydrogenase | - |
Faxonius virilis |
LDH | - |
Faxonius virilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Faxonius virilis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the enzyme from aerobic control muscle has a significantly higher melting temperature (greater thermal stability) compared to the anoxic enzyme form, suggesting that there is a structural difference between the two enzyme forms. Both anoxic and control LDH are most thermally stable around pH 7.6 although the difference in TM between pH 7.3 and pH 7.6 is not significant for the anoxic LDH | Faxonius virilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at, pyruvate reduction | Faxonius virilis |
8.5 | - |
assay at, (S)-lactate oxidation | Faxonius virilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Faxonius virilis | |
NADH | - |
Faxonius virilis |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
20.4 | - |
anoxic enzyme, pH 7.2, 25°C | Faxonius virilis | pyruvate | |
30.3 | - |
aerobic control enzyme, pH 7.2, 25°C | Faxonius virilis | pyruvate |
General Information | Comment | Organism |
---|---|---|
physiological function | lactate dehydrogenase is the terminal enzyme of anaerobic glycolysis, and has a crucial role in sustaining ATP production by glycolysis during periods of anoxia via regenerating NAD+ through the production of lactate. Anoxia-induced modifications of crayfish muscle LDH may contribute significantly to modulating enzyme function under anoxic conditions | Faxonius virilis |