A dual L-glucose/L-galactose catabolic pathway in <i>Luteolibacter</i> species strain LG18.

ABSTRACT: The L-glucose catabolic pathway of Luteolibacter sp. strain LG18 was determined. L-glucose dehydrogenase (LguA) and L-gluconate dehydrogenase (LguD), purified from the cell extract of strain LG18, convert L-glucose to 5-keto-L-gluconate via L-gluconate, and these recombinant enzymes also utilize L-galactose and L-galactonate, respectively. Genes encoding these enzymes are both located in the gene cluster, lguABCDEF, which includes other genes possibly involved in L-galactose catabolism. After oxidation of L-gluconate, 5-keto-L-gluconate is converted to D-tagaturonate by LguG, a C-4 epimerase, determined with the recombinant enzyme. The subsequent LG18 reactions are likely to proceed in the same way as Escherichia coli L-galactonate catabolism, wherein LguC reduces C-5

SUBMITTER: Yachida M 

PROVIDER: S-EPMC12632266 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature