This mycobacterial enzyme catalyses the acylation of 2-O-sulfo-α,α-trehalose at the 2′ position by a C16 or C18 fatty acyl group during the biosynthesis of mycobacterial sulfolipids.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
This mycobacterial enzyme catalyses the acylation of 2-O-sulfo-alpha,alpha-trehalose at the 2' position by a C16 or C18 fatty acyl group during the biosynthesis of mycobacterial sulfolipids.
deletion of PapA2 gene abolishes sulfolipid-I production. Both acyltransferases PapA1 and PapA2 are required for all acylation steps of sulfolipid-I assembly
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
acyltransferases PapA2 and PapA1 are responsible for the sequential acylation of trehalose-2-sulfate to form diacetylated intermediate SL1278 and are essential for sulfolipid SL-1 biosynthesis. In vitro, recombinant PapA2 converts T2S to 2'-palmitoyl T2S, and PapA1 further elaborates this SL-1 intermediate to an analog of SL1278. Disruption of PapA2 and PapA1 genes results in loss of SL-1 (and SL1278). The deletions do not appear to affect bacterial replication, trafficking or virulence
deletion of PapA2 gene abolishes sulfolipid-I production. Both acyltransferases PapA1 and PapA2 are required for all acylation steps of sulfolipid-I assembly
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
acyltransferases PapA2 and PapA1 are responsible for the sequential acylation of trehalose-2-sulfate to form diacetylated intermediate SL1278 and are essential for sulfolipid SL-1 biosynthesis. In vitro, recombinant PapA2 converts T2S to 2'-palmitoyl T2S, and PapA1 further elaborates this SL-1 intermediate to an analog of SL1278. Disruption of PapA2 and PapA1 genes results in loss of SL-1 (and SL1278). The deletions do not appear to affect bacterial replication, trafficking or virulence
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