{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T12:18:54Z","timestamp":1789906734654,"version":"4.0.1"},"reference-count":61,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2011,8,23]],"date-time":"2011-08-23T00:00:00Z","timestamp":1314057600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2011,9]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p><jats:italic>Mycobacterium tuberculosis<\/jats:italic> accumulates large amounts of triacylglycerol (TAG) which acts as storage compounds for energy and carbon. The mycobacterial triacylglycerols stored in the form of intracellular lipid droplets are essential for long\u2010term survival of <jats:italic>M.\u2003tuberculosis<\/jats:italic> during a dormant state. We report here that when the <jats:italic>M.\u2003tuberculosis<\/jats:italic> mycolytransferase Ag85A is overexpressed in <jats:italic>Mycobacterium smegmatis<\/jats:italic> mc<jats:sup>2<\/jats:sup>155, cell morphology was changed and the cells became grossly enlarged. A massive formation of lipid bodies and a change in lipid pattern was observed simultaneously. We suspected a possible role of Ag85A in the acyl lipid metabolism and discovered that the enzyme possesses acyl\u2010CoA:diacylglycerol acyltransferase (DGAT) activity in addition to its well\u2010known function as mycolyltransferase. Ag85A mediates the transesterification of diacylglycerol using long\u2010chain acyl\u2010CoA as acyl donors. The <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> and <jats:italic>K<\/jats:italic><jats:sub>cat<\/jats:sub> values for palmitoleoyl\u2010coenzyme A were 390\u2003\u00b5M and 55.54\u2003min<jats:sup>\u22121<\/jats:sup> respectively. A docking model suggests that palmitoleoyl\u2010coenzyme A and 1,2\u2010dipalmitin occupy the same active site as trehalose 6,6\u2032\u2010dimycolate and trehalose 6\u2032\u2010monomycolate. The site\u2010directed Ser126Ala mutation of the active site proved that this residue is involved in the catalytic activity of this enzyme. Although not proven conclusively for dormant stage of <jats:italic>M.\u2003tuberculosis<\/jats:italic>, our novel finding about the synthesis of TAGs by Ag85A strongly suggests that Ag85A may play a significant role in the formation of lipid storage bodies and thus also in the establishment and maintenance of a persistent tuberculosis infection.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2011.07792.x","type":"journal-article","created":{"date-parts":[[2011,8,8]],"date-time":"2011-08-08T09:19:24Z","timestamp":1312795164000},"page":"1577-1592","source":"Crossref","is-referenced-by-count":63,"title":["The <i>Mycobacterium tuberculosis<\/i> Ag85A is a novel diacylglycerol acyltransferase involved in lipid body formation"],"prefix":"10.1111","volume":"81","author":[{"given":"Ayssar 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