Francisella tularensis is a highly communicable gram-negative bacterium and the etiological cause of the ferile disease, tularemia. Amongst the proteins essential to the pathogenicity of F. tularensis is the putative esterase FTT941c. FTT941c has sequence similarity to serine hydrolases and a canonical GxSxG catalytic motif, but no highly homologous enzymes (>30%) are known. To confirm its esterase activity and measure its substrate specificity, FTT941c was expressed heterologously, purified to homogeneity, and characterized for substrate specificity. The substrate specificity was determined using substrates with varying carbon chain lengths, polarity, steric hindrance, and aromaticity. FTT941c showed broad substrate specificity catalyzing reactions with alkyl chains from C2-C12 with a slight preference for C4. FTT941c was also active against sterically constrained ester bonds with alkyl, cycloalkyl, aromatic, unsaturated, ether, and fluorine R-groups. The broad substrate specificity of FTT941c makes identification of its cellular activity difficult, but suggests its potential use as a broad biocatalyst.

Purification and characterization of FTT941c, a putative essential esterase from <i>Francisella tularensis</i>

243rd National Meeting (2012)

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Purification and characterization of FTT941c, a putative essential esterase from Francisella tularensis