1421868-74-7Relevant articles and documents
Synthesis, structural elucidation, and biochemical analysis of immunoactive glucuronosyl diacylglycerides of mycobacteria and corynebacteria
Cao, Benjamin,Chen, Xingqiang,Yamaryo-Botte, Yoshiki,Richardson, Mark B.,Martin, Kirstee L.,Khairallah, George N.,Rupasinghe, Thusita W.T.,O'Flaherty, Roisin M.,O'Hair, Richard A.J.,Ralton, Julie E.,Crellin, Paul K.,Coppel, Ross L.,McConville, Malcolm J.,Williams, Spencer J.
, p. 2175 - 2190 (2013)
Glucuronosyl diacylglycerides (GlcAGroAc2) are functionally important glycolipids and membrane anchors for cell wall lipoglycans in the Corynebacteria. Here we describe the complete synthesis of distinct acyl-isoforms of GlcAGroAc2 bearing both acylation patterns of (R)-tuberculostearic acid (C19:0) and palmitic acid (C 16:0) and their mass spectral characterization. Collision-induced fragmentation mass spectrometry identified characteristic fragment ions that were used to develop rules allowing the assignment of the acylation pattern as C19:0 (sn-1), C16:0 (sn-2) in the natural product from Mycobacterium smegmatis, and the structural assignment of related C18:1 (sn-1), C16:0 (sn-2) GlcAGroAc2 glycolipids from M. smegmatis and Corynebacterium glutamicum. A synthetic hydrophobic octyl glucuronoside was used to characterize the GDP-mannose-dependent mannosyltransferase MgtA from C. glutamicum that extends GlcAGroAc2. This enzyme is an Mg2+/Mn2+- dependent metalloenzyme that undergoes dramatic activation upon reduction with dithiothreitol.
