(2R)-3-sulfolactate dehydrogenase (SLDH)

(2R)-3-sulfolactate dehydrogenase (SLDH) is a bacterial and archaeal enzyme that plays a critical role in the catabolism of organosulfonates, such as sulfoquinovose and taurine-derived intermediates. It catalyzes the reversible NAD(P)+-dependent oxidation of 3-sulfolactate to 3-sulfopyruvate, a key step in pathways that allow microorganisms to extract energy and sulfur from sulfonated compounds abundant in plants and algae. In the human context, SLDH is found in specific members of the gut microbiota where its activity contributes to the production of downstream metabolites like hydrogen sulfide, which has complex implications for intestinal health and systemic metabolism. While it is not a direct target for current human pharmaceuticals, SLDH is an emerging focus in microbiome research due to its association with conditions such as obesity and inflammatory bowel disease. Structurally, SLDH is distinct from common dehydrogenases as it lacks the traditional Rossmann fold, making it a unique model for studying non-canonical oxidoreductase mechanisms.

Other names

3-sulfolactate dehydrogenase(R)-sulfolactate dehydrogenase(S)-sulfolactate dehydrogenaseL-sulfolactate dehydrogenaseComCSlcDDhpASlaB

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