EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.27 | additional information | thermodynamic activation parameters, overview | Champsocephalus gunnari | |
1.1.1.27 | additional information | thermodynamic activation parameters, overview | Deinococcus radiodurans | |
1.1.1.27 | additional information | thermodynamic activation parameters, overview | Thermus thermophilus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.27 | expression in Escherichia coli strain DH5alpha | Deinococcus radiodurans |
1.1.1.27 | expression in Escherichia coli strain DH5alpha | Thermus thermophilus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.27 | 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 |
1.1.1.27 | apo enzyme form, X-ray diffraction structure determination and analysis at 2.35 A resolution, molecular replacement | Champsocephalus gunnari |
1.1.1.27 | 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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.27 | additional information | - |
additional information | an allosteric enzyme | Deinococcus radiodurans | |
1.1.1.27 | 0.16 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Champsocephalus gunnari | |
1.1.1.27 | 0.16 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Thermus thermophilus | |
1.1.1.27 | 0.21 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Deinococcus radiodurans |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.27 | 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 | |
1.1.1.27 | 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 | |
1.1.1.27 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.27 | Champsocephalus gunnari | O93541 | - |
- |
1.1.1.27 | Deinococcus radiodurans | P50933 | - |
- |
1.1.1.27 | Thermus thermophilus | Q5SJA1 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.27 | native enzyme by ultracentrifugation, hydrophobic interaction chromatography, gel filtration, and ultrafiltration | Champsocephalus gunnari |
1.1.1.27 | 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 |
1.1.1.27 | 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 |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.1.1.27 | additional information | structural features for structural stability, comparison to enzymes from other species in extreme environments | Champsocephalus gunnari | - |
1.1.1.27 | additional information | structural features for structural stability, comparison to enzymes from other species in extreme environments | Deinococcus radiodurans | - |
1.1.1.27 | additional information | structural features for structural stability, comparison to enzymes from other species in extreme environments | Thermus thermophilus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.27 | 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 | |
1.1.1.27 | 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 | |
1.1.1.27 | 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 | |
1.1.1.27 | pyruvate + NADH + H+ | active site structure and substrate binding, overview | Champsocephalus gunnari | (S)-lactate + NAD+ | - |
r | |
1.1.1.27 | pyruvate + NADH + H+ | active site structure and substrate binding, overview | Deinococcus radiodurans | (S)-lactate + NAD+ | - |
r | |
1.1.1.27 | pyruvate + NADH + H+ | active site structure and substrate binding, overview | Thermus thermophilus | (S)-lactate + NAD+ | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.27 | More | primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from crystal structure, overview | Deinococcus radiodurans |
1.1.1.27 | More | primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview | Champsocephalus gunnari |
1.1.1.27 | More | primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview | Thermus thermophilus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.27 | lactate dehydrogenase | - |
Champsocephalus gunnari |
1.1.1.27 | lactate dehydrogenase | - |
Deinococcus radiodurans |
1.1.1.27 | lactate dehydrogenase | - |
Thermus thermophilus |
1.1.1.27 | LDH | - |
Champsocephalus gunnari |
1.1.1.27 | LDH | - |
Deinococcus radiodurans |
1.1.1.27 | LDH | - |
Thermus thermophilus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.27 | 50 | - |
- |
Deinococcus radiodurans |
1.1.1.27 | 90 | - |
about | Thermus thermophilus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.27 | 45 | - |
inactivation above, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments | Champsocephalus gunnari |
1.1.1.27 | 60 | - |
stable up to, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments | Deinococcus radiodurans |
1.1.1.27 | 90 | - |
stable up to, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments | Thermus thermophilus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.27 | 230 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Champsocephalus gunnari | |
1.1.1.27 | 676 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Thermus thermophilus | |
1.1.1.27 | 884 | - |
pyruvate | pH 7.0, 0°C, recombinant enzyme | Deinococcus radiodurans |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.27 | 7 | - |
the enzyme shows a narrow pH optimum | Deinococcus radiodurans |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.27 | additional information | - |
pH profile | Champsocephalus gunnari |
1.1.1.27 | additional information | - |
pH profile | Deinococcus radiodurans |
1.1.1.27 | additional information | - |
pH profile | Thermus thermophilus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.27 | NAD+ | - |
Champsocephalus gunnari | |
1.1.1.27 | NAD+ | - |
Deinococcus radiodurans | |
1.1.1.27 | NAD+ | - |
Thermus thermophilus | |
1.1.1.27 | NADH | - |
Champsocephalus gunnari | |
1.1.1.27 | NADH | - |
Deinococcus radiodurans | |
1.1.1.27 | NADH | - |
Thermus thermophilus |