3-keto-L-gulonate 6-phosphate decarboxylase (UlaD)

3-keto-L-gulonate 6-phosphate decarboxylase (UlaD) is a bacterial enzyme that plays a critical role in the anaerobic catabolism of L-ascorbate (Vitamin C) [UniProt]. It catalyzes the conversion of 3-keto-L-gulonate 6-phosphate into L-xylulose 5-phosphate and carbon dioxide, a reaction that allows bacteria to utilize ascorbate as a carbon and energy source under oxygen-limited conditions [PubMed]. The enzyme is a member of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily and requires divalent metal ions, such as magnesium or manganese, for its catalytic function [PubMed]. While it is found in various enteric bacteria like Escherichia coli, the entire L-ascorbate utilization pathway is absent in humans, making the enzyme a potential target for narrow-spectrum antimicrobials [Journal of Biological Chemistry]. Such inhibitors could theoretically disrupt the fitness of pathogenic bacteria in the human gut without affecting host metabolism [Journal of Bacteriology]. Currently, there are no approved drugs or clinical-stage compounds that target this enzyme, and it remains primarily a subject of research in microbial biochemistry and structural biology [PubMed].

Other names

UlaD3-oxo-L-gulonate 6-phosphate decarboxylaseSgbDKGPDCL-ascorbate-6-phosphate catabolism protein D

No known therapeutic drugs; the enzyme naturally catalyzes the decarboxylation of 3-keto-L-gulonate 6-phosphate to L-xylulose 5-phosphate.