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Literature summary for 1.1.1.27 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

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(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain DH5alpha Deinococcus radiodurans
expression in Escherichia coli strain DH5alpha Thermus thermophilus

Crystallization (Commentary)

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Champsocephalus gunnari O93541
-
-
Deinococcus radiodurans P50933
-
-
Thermus thermophilus Q5SJA1
-
-

Purification (Commentary)

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

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 and Products (Substrate)

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

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Deinococcus radiodurans
90
-
about Thermus thermophilus

Temperature Stability [°C]

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 [1/s]

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

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

pH Range

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

Cofactor Comment Organism Structure
NAD+
-
Champsocephalus gunnari
NAD+
-
Deinococcus radiodurans
NAD+
-
Thermus thermophilus
NADH
-
Champsocephalus gunnari
NADH
-
Deinococcus radiodurans
NADH
-
Thermus thermophilus