D-lactate dehydrogenase (quinone) (D-iLDH)

Bacterial membrane-bound D-lactate dehydrogenase (D-iLDH), specifically the quinone-dependent form (EC 1.1.5.12), is a flavoprotein essential for the utilization of D-lactate as a primary carbon and energy source in many bacteria (UniProt: P00361). It is located on the cytoplasmic surface of the inner membrane and facilitates the oxidation of D-lactate to pyruvate, transferring electrons directly to the respiratory quinone pool (PubMed: 15686558). This process is vital for maintaining the proton motive force and ATP production in pathogens like Escherichia coli and Staphylococcus aureus (PubMed: 28844881). Since humans primarily utilize L-lactate and possess a structurally distinct mitochondrial D-lactate dehydrogenase, this bacterial enzyme represents a promising target for narrow-spectrum antibiotics (PubMed: 31265111). Inhibiting D-iLDH can effectively starve bacteria of energy in lactate-rich environments, such as abscesses or the gut (PubMed: 25631484). Current therapeutic research focuses on small-molecule inhibitors that can selectively bind the bacterial enzyme's active site without cross-reacting with human metabolic pathways (PubMed: 18439557).

Other names

Bacterial membrane-bound D-lactate dehydrogenaseD-lactate:quinone oxidoreductaseD-LDHD-lactate ferricytochrome c oxidoreductasedld

Inhibition of the oxidation of D-lactate to pyruvate, which prevents electron transfer to the quinone pool, thereby disrupting the bacterial respiratory chain and ATP generation (PubMed: 28844881).