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

Abstract : 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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Submitted on : Tuesday, December 14, 2021 - 10:32:31 AM
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Jihen Ati, Cyril Colas, Pierre Lafite, Ryan Sweeney, Ruixiang Blake Zheng, et al.. The LPG1x family from $Leishmania\ major$ is constituted of rare eukaryotic galactofuranosyltransferases with unprecedented catalytic properties. Scientific Reports, Nature Publishing Group, 2018, 8, pp.147566. ⟨10.1038/s41598-018-35847-w⟩. ⟨hal-03478310⟩

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