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Literature summary for 2.4.1.345 extracted from

  • Guerin, M.E.; Kaur, D.; Somashekar, B.S.; Gibbs, S.; Gest, P.; Chatterjee, D.; Brennan, P.J.; Jackson, M.
    New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB is an essential enzyme of Mycobacterium smegmatis (2009), J. Biol. Chem., 284, 25687-25696.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0QWG6
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Mycolicibacterium smegmatis ATCC 700084 A0QWG6
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General Information

General Information Comment Organism
physiological function both mannosyltransferases PimA and PimB' (MSMEG_4253) recognize phosphatidyl-myo-inositol as a lipid acceptor. PimA specifically catalyzes the transfer of a mannopyranosyl residue to the 2-position of the myo-inositol ring of phosphatidylinositol, whereas PimB' exclusively transfers to the 6-position. PimB' can catalyze the transfer of a mannopyranosyl residue onto the phosphatidylinositol-monomannoside (PIM1) product of PimA, while PimA is unable in vitro to transfer mannopyranosyl onto the PIM1 product of PimB' Mycolicibacterium smegmatis