The enzyme is an FAD-dependent peripheral membrane dehydrogenase that participates in respiration. Electrons derived from D-lactate oxidation are transferred to the membrane soluble quinone pool.
Specify your search results
The enzyme appears in viruses and cellular organisms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(R)-lactate:quinone 2-oxidoreductase
The enzyme is an FAD-dependent peripheral membrane dehydrogenase that participates in respiration. Electrons derived from D-lactate oxidation are transferred to the membrane soluble quinone pool.
not active with D-glycerate, L-glycerate, succinate, malate, D-tartrate, L-tartrate, meso-tartrate, 1-propanol, or isopropanol as substrates and oxidized diphosphopyridine nucleotide has no effect on the catalytic conversion of D-lactate to pyruvate
not active with D-glycerate, L-glycerate, succinate, malate, D-tartrate, L-tartrate, meso-tartrate, 1-propanol, or isopropanol as substrates and oxidized diphosphopyridine nucleotide has no effect on the catalytic conversion of D-lactate to pyruvate
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
inactivation of Dld results in the loss of the ability to grow with D-lactate. Heterologous expression in Corynebacterium efficiens enables this species to grow with D-lactate as sole carbon source
inactivation of Dld results in the loss of the ability to grow with D-lactate. Heterologous expression in Corynebacterium efficiens enables this species to grow with D-lactate as sole carbon source
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fluorine-19 nuclear magnetic resonance spectroscopy of 5-fluorotryptophan-labeled enzyme. The membrane-bound D-lactate dehydrogenase may have the two-domain structure of many cytoplasmic dehydrogenases but with the addition of a membrane-binding domain between the catalytic and cofactor-binding domains
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
Peersen, O.; Pratt, E.; Truong, H.; Ho, C.; Rule, G.
Site-specific incorporation of 5-fluorotryptophan as a probe of the structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli: A19F nuclear magnetic resonance study
HOME
login
history
all enzymes
BRENDA home
History
1.1.5.12 D-lactate dehydrogenase (quinone)
more
top
Information
