In this section, you can access to the latest technical information related to the FUTURE project topic.

Identification and biochemical characterization of a novel ?-1,3-mannosyltransferase WfcD from Escherichia coli O141

Glycosyltransferases (GTs) catalyze the formation of regio- and stereospecific glycosidic linkages between specific sugar donors and recipients. In this study, the function of the wfcD gene from the Escherichia coli O141 O-antigen gene cluster encoding an ?-1,3-mannosyltransferase that catalyzed the formation of the linkage Man(?1-3)-GlcNAc was biochemically characterized. WfcD was expressed in E. coli BL21 (DE3), and the enzymatic product was identified by liquid chromatography-mass spectrometry (LC-MS), collision-induced dissociation electrospray ionization ion trap multiple tandem MS (CID-ESI-IT-MSn) and glycosidase digestion using the donor substrate GDP-Man and the synthetic acceptor substrate decyl diphosphate 2-acetamido-2-deoxy-?-D-glucopyranose (GlcNAc-PP-De). The kinetic and physiochemical properties and the substrate specificity of WfcD were investigated. WfcD is the first characterized bacterial mannosyltransferase that acts on the Man(?1-3)-GlcNAc linkage. This study enhances our knowledge of the diverse functions of GTs.

» Author: Chao Chen, Xi Hou, Natalia Utkina, Leonid Danilov, Dawei Zhou, Vladimir Torgov, Vladimir Veselovsky, Bin Liu, Lu Feng

» Reference: Carbohydrate Research

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