Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | thermodynamic activation parameters, overview | Champsocephalus gunnari | |
additional information | thermodynamic activation parameters, overview | Deinococcus radiodurans | |
additional information | thermodynamic activation parameters, overview | Thermus thermophilus |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli strain DH5alpha | Deinococcus radiodurans |
expression in Escherichia coli strain DH5alpha | Thermus thermophilus |
Crystallization (Comment) | Organism |
---|---|
apo enzyme form and enzyme in ternary complex, X-ray diffraction structure determination and analysis at 2.1-2.3 A resolution, molecular replacement | Thermus thermophilus |
apo enzyme form, X-ray diffraction structure determination and analysis at 2.35 A resolution, molecular replacement | Champsocephalus gunnari |
purified enzyme, hanging drop vapor diffusion technique, 8 mg/ml protein in 20% PEG 5000 MME, 0.1M bicine, pH 9.0, at room temperature, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement | Deinococcus radiodurans |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | an allosteric enzyme | Deinococcus radiodurans | |
0.16 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Champsocephalus gunnari | |
0.16 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Thermus thermophilus | |
0.21 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Deinococcus radiodurans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate + NADH + H+ | Champsocephalus gunnari | LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis | (S)-lactate + NAD+ | - |
r | |
pyruvate + NADH + H+ | Deinococcus radiodurans | LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis | (S)-lactate + NAD+ | - |
r | |
pyruvate + NADH + H+ | Thermus thermophilus | LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis | (S)-lactate + NAD+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Champsocephalus gunnari | O93541 | - |
- |
Deinococcus radiodurans | P50933 | - |
- |
Thermus thermophilus | Q5SJA1 | - |
- |
Purification (Comment) | Organism |
---|---|
native enzyme by ultracentrifugation, hydrophobic interaction chromatography, gel filtration, and ultrafiltration | Champsocephalus gunnari |
recombinant enzyme from Escherichia coli strain DH5alpha by heat treatment at 55°C for 90 s, hydrophobic interaction chromatography, hydroxyapatite chromatography, gel filtration, and ultrafiltration | Deinococcus radiodurans |
recombinant enzyme from Escherichia coli strain DH5alpha by heat treatment at 70°C for 90 s, anion exchange chromatography, gel filtration, and ultrafiltration | Thermus thermophilus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | structural features for structural stability, comparison to enzymes from other species in extreme environments | Champsocephalus gunnari | - |
additional information | structural features for structural stability, comparison to enzymes from other species in extreme environments | Deinococcus radiodurans | - |
additional information | structural features for structural stability, comparison to enzymes from other species in extreme environments | Thermus thermophilus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate + NADH + H+ | LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis | Champsocephalus gunnari | (S)-lactate + NAD+ | - |
r | |
pyruvate + NADH + H+ | LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis | Deinococcus radiodurans | (S)-lactate + NAD+ | - |
r | |
pyruvate + NADH + H+ | LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis | Thermus thermophilus | (S)-lactate + NAD+ | - |
r | |
pyruvate + NADH + H+ | active site structure and substrate binding, overview | Champsocephalus gunnari | (S)-lactate + NAD+ | - |
r | |
pyruvate + NADH + H+ | active site structure and substrate binding, overview | Deinococcus radiodurans | (S)-lactate + NAD+ | - |
r | |
pyruvate + NADH + H+ | active site structure and substrate binding, overview | Thermus thermophilus | (S)-lactate + NAD+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from crystal structure, overview | Deinococcus radiodurans |
More | primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview | Champsocephalus gunnari |
More | primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview | Thermus thermophilus |
Synonyms | Comment | Organism |
---|---|---|
lactate dehydrogenase | - |
Champsocephalus gunnari |
lactate dehydrogenase | - |
Deinococcus radiodurans |
lactate dehydrogenase | - |
Thermus thermophilus |
LDH | - |
Champsocephalus gunnari |
LDH | - |
Deinococcus radiodurans |
LDH | - |
Thermus thermophilus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
- |
Deinococcus radiodurans |
90 | - |
about | Thermus thermophilus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
inactivation above, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments | Champsocephalus gunnari |
60 | - |
stable up to, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments | Deinococcus radiodurans |
90 | - |
stable up to, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments | Thermus thermophilus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
230 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Champsocephalus gunnari | |
676 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Thermus thermophilus | |
884 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Deinococcus radiodurans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
the enzyme shows a narrow pH optimum | Deinococcus radiodurans |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
pH profile | Champsocephalus gunnari |
additional information | - |
pH profile | Deinococcus radiodurans |
additional information | - |
pH profile | Thermus thermophilus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Champsocephalus gunnari | |
NAD+ | - |
Deinococcus radiodurans | |
NAD+ | - |
Thermus thermophilus | |
NADH | - |
Champsocephalus gunnari | |
NADH | - |
Deinococcus radiodurans | |
NADH | - |
Thermus thermophilus |