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Literature summary extracted from

  • Ostendorp, R.; Auerbach, G.; Jaenicke, R.
    Extremely thermostable L(+)-lactate dehydrogenase from Thermotoga maritima: cloning, characterization, and crystallization of the recombinant enzyme in its tetrameric and octameric state (1996), Protein Sci., 5, 862-873.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.27 expression in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.27
-
 Thermotoga maritima

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.27 0.018
-
 pyruvate octameric enzyme form Thermotoga maritima
1.1.1.27 0.019
-
 pyruvate tetrameric enzyme form Thermotoga maritima

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.27 35000
-
 8 * 35000, enzyme also exists in an tetrameric enzyme form, SDS-PAGE, meniscus depletion experiments in 4 M guanidinium chloride Thermotoga maritima
1.1.1.27 140000
-
 tetramer, gel filtration Thermotoga maritima
1.1.1.27 269300
-
 meniscus depletion experiments Thermotoga maritima
1.1.1.27 280000
-
 octamer, gel filtration Thermotoga maritima
1.1.1.27 280900
-
 equilibrium sedimentation Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Thermotoga maritima
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.27
-
 Thermotoga maritima

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.27 additional information
-
-
 Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.27 pyruvate + NADH + H+
-
 Thermotoga maritima (S)-lactate + NAD+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.27 octamer 8 * 35000, enzyme also exists in an tetrameric enzyme form, SDS-PAGE, meniscus depletion experiments in 4 M guanidinium chloride Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 NADH coenzyme Thermotoga maritima