The LPG1x family from $Leishmania\ major$ is constituted of rare eukaryotic galactofuranosyltransferases with unprecedented catalytic properties
Résumé
Galactofuranosyltransferases are poorly described enzymes despite their crucial role in the virulence
and the pathogenicity of numerous microorganisms. These enzymes are considered as potential
targets for therapeutic action. In addition to the only well-characterised prokaryotic GlfT2 from
Mycobacterium tuberculosis, four putative genes in Leishmania major were previously described
as potential galactofuranosyltransferases. In this study, we have cloned, over-expressed, purifed
and fully determined the kinetic parameters of these four eukaryotic enzymes, thus demonstrating
their unique potency in catalysing the transfer of the galactofuranosyl moiety into acceptors. Their
individual promiscuity revealed to be diferent, as some of them could efciently use NDP-pyranoses
as donor substrates in addition to the natural UDP-galactofuranose. Such results pave the way for the
development of chemoenzymatic synthesis of furanosyl-containing glycoconjugates as well as the
design of improved drugs against leishmaniasis.
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