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Literature summary for 2.3.1.288 extracted from

  • Seeliger, J.C.; Holsclaw, C.M.; Schelle, M.W.; Botyanszki, Z.; Gilmore, S.A.; Tully, S.E.; Niederweis, M.; Cravatt, B.F.; Leary, J.A.; Bertozzi, C.R.
    Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis (2012), J. Biol. Chem., 287, 7990-8000 .
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-associated Mycobacterium tuberculosis 16020
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Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WIK7
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Mycobacterium tuberculosis ATCC 25618 P9WIK7
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General Information

General Information Comment Organism
physiological function sulfolipid SL-1 biosynthesis is initiated by sulfotransferase by sulfating the abundant disaccharide trehalose to form T2S. The acyltransferase PapA2 then catalyzes the esterification of T2S at the 2'-position to generate a monoacylated intermediate. The polyketide synthase Pks2 synthesizes methyl-branched (hydroxy)phthioceranoyl chains. PapA1 transfers the product of Pks2 to the 3'-position of the monoacylated intermediate, yielding adiacylated species. Additional acylations at the 6- and 6'-positions produce fully elaborated SL-1 Mycobacterium tuberculosis