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Literature summary extracted from

  • Pratt, E.; Fung, L.; Flower, J.; Ho, C.
    Membrane-bound D-lactate dehydrogenase from Escherichia coli: Purification and properties (1979), Biochemistry, 18, 312-316.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.5.12 Triton X-100 5fold increase in activtiy of purified detergent-free enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.12 0.4
-
 (R)-lactate pH 8.0, 23°C Escherichia coli
1.1.5.12 0.4
-
 (R)-lactate presence of Triton X-100, pH 8.0, 23°C Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.12 membrane
-
 Escherichia coli 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.5.12 75000
-
 x * 75000, SDS-PAGE Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.12 Escherichia coli
-
-
-
1.1.5.12 Escherichia coli W3110trpA33
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.12 from sonicated cell extracts, purifiaction in the presence of 1% Triton X-100 and 0.1% sodium dodecyl sulfate Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.5.12 230
-
 pH 8.0, 23°C Escherichia coli

Storage Stability

EC Number Storage Stability Organism
1.1.5.12 -20°C, detergent-free enzyme is destroyed by freezing and thawing Escherichia coli
1.1.5.12 4°C, stable up to 6 months Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.12 (R)-lactate + oxidized phenazine methosulfate
-
 Escherichia coli pyruvate + reduced phenazine methosulfate
-
 ?
1.1.5.12 (R)-lactate + oxidized phenazine methosulfate
-
 Escherichia coli W3110trpA33 pyruvate + reduced phenazine methosulfate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.5.12 ? x * 75000, SDS-PAGE Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.5.12 60
-
 1 h, 35% loss of activity, more readily inactivated in presence of Triton X-100 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.5.12 9 9.5
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.12 FAD visible absorption spectrum of the purified enzyme shows a broad peak at around 450 nm and a shoulder at around 480 nm Escherichia coli