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Literature summary for 1.1.1.27 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)

Cloned (Comment) Organism
expression in Escherichia coli Thermotoga maritima

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Thermotoga maritima

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermotoga maritima

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

Cofactor Comment Organism Structure
NADH coenzyme Thermotoga maritima