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Literature summary for 1.1.5.12 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
Search for more literature for 1.1.5.12

Activating Compound

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

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli W3110trpA33
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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]

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 9.5
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
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