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  • Title: High-resolution structures of Lactobacillus salivarius transketolase in the presence and absence of thiamine pyrophosphate.
    Author: Lukacik P, Lobley CM, Bumann M, Arena de Souza V, Owens RJ, O'Toole PW, Walsh MA.
    Journal: Acta Crystallogr F Struct Biol Commun; 2015 Oct; 71(Pt 10):1327-34. PubMed ID: 26457526.
    Abstract:
    Probiotic bacterial strains have been shown to enhance the health of the host through a range of mechanisms including colonization, resistance against pathogens, secretion of antimicrobial compounds and modulation of the activity of the innate immune system. Lactobacillus salivarius UCC118 is a well characterized probiotic strain which survives intestinal transit and has many desirable host-interaction properties. Probiotic bacteria display a wide range of catabolic activities, which determine their competitiveness in vivo. Some lactobacilli are heterofermentative and can metabolize pentoses, using a pathway in which transketolase and transaldolase are key enzymes. L. salivarius UCC118 is capable of pentose utilization because it encodes the key enzymes on a megaplasmid. The crystal structures of the megaplasmid-encoded transketolase with and without the enzyme cofactor thiamine pyrophosphate have been determined. Comparisons with other known transketolase structures reveal a high degree of structural conservation in both the catalytic site and the overall conformation. This work extends structural knowledge of the transketolases to the industrially and commercially important Lactobacillus genus.
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