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Literature summary extracted from

  • Matsushita, K., Kaback, H.R.
    D-Lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome O oxidase (1986), Biochemistry, 25, 2321-2327.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.12 Escherichia coli
-
-
-
1.1.5.12 Escherichia coli GR19N
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.12
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.12 D-lactate + ferricyanide
-
 Escherichia coli pyruvate + ferrocyanide
-
 ?
1.1.5.12 D-lactate + ferricyanide
-
 Escherichia coli GR19N pyruvate + ferrocyanide
-
 ?
1.1.5.12 D-lactate + ubiquinone 1
-
 Escherichia coli pyruvate + reduced ubiquinone 1
-
 ?
1.1.5.12 D-lactate + ubiquinone 1
-
 Escherichia coli GR19N pyruvate + reduced ubiquinone 1
-
 ?

General Information

EC Number General Information Comment Organism
1.1.5.12 physiological function D-lactate/ubiquinone 1 or D-lactate/ferricyanide oxidoreductase activity does not generate a membranepotential, suggesting that electron flow from D-lactate dehydrogenase to ubiquinone is not electrogenic. Proteoliposomes reconstituted with purified D-lactate dehydrogenase, ubiquinone 8, and purified cytochrome o catalyze D-lactate and ubiquinol 1 oxidation and generate a H+ electrochemical gradient similar to that observed in membrane vesicles. The only component between D-lactate dehydrogenase or ubiquinol and oxygen in the membranes that is directly involved in the generation of the H+ electrochemical gradient is cytochrome 0 Escherichia coli