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Literature summary extracted from

  • Coquelle, N.; Fioravanti, E.; Weik, M.; Vellieux, F.; Madern, D.
    Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments (2007), J. Mol. Biol., 374, 547-562.
    View publication on PubMed

Activating Compound

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

Cloned(Commentary)

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

Crystallization (Commentary)

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

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
-
-

Purification (Commentary)

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

Source Tissue

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
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.27 7
-
the enzyme shows a narrow pH optimum Deinococcus radiodurans

pH Range

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

Cofactor

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