The LPG1x family from $Leishmania\ major$ is constituted of rare eukaryotic galactofuranosyltransferases with unprecedented catalytic properties

International audienceGalactofuranosyltransferases are poorly described enzymes despite their crucial role in the virulenceand the pathogenicity of numerous microorganisms. These enzymes are considered as potentialtargets for therapeutic action. In addition to the only well-characterised prokaryotic GlfT2 fromMycobacterium tuberculosis, four putative genes in Leishmania major were previously describedas potential galactofuranosyltransferases. In this study, we have cloned, over-expressed, purifedand fully determined the kinetic parameters of these four eukaryotic enzymes, thus demonstratingtheir unique potency in catalysing the transfer of the galactofuranosyl moiety into acceptors. Theirindividual promiscuity revealed to be diferent, as some of them could efciently use NDP-pyranosesas donor substrates in addition to the natural UDP-galactofuranose. Such results pave the way for thedevelopment of chemoenzymatic synthesis of furanosyl-containing glycoconjugates as well as thedesign of improved drugs against leishmaniasis