Identification and biochemical characterization of a novel α-1,3-mannosyltransferase WfcD from Escherichia coli O141
Copyright © 2017 Elsevier Ltd. All rights reserved..
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 α-1,3-mannosyltransferase that catalyzed the formation of the linkage Man(α1-3)-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-α-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(α1-3)-GlcNAc linkage. This study enhances our knowledge of the diverse functions of GTs.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2017 |
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Erschienen: |
2017 |
Enthalten in: |
Zur Gesamtaufnahme - volume:443-444 |
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Enthalten in: |
Carbohydrate research - 443-444(2017) vom: 18. Apr., Seite 78-86 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Chen, Chao [VerfasserIn] |
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Date Completed 26.12.2017 Date Revised 26.12.2017 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1016/j.carres.2017.04.003 |
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PPN (Katalog-ID): |
NLM270902325 |
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520 | |a Copyright © 2017 Elsevier Ltd. All rights reserved. | ||
520 | |a 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 α-1,3-mannosyltransferase that catalyzed the formation of the linkage Man(α1-3)-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-α-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(α1-3)-GlcNAc linkage. This study enhances our knowledge of the diverse functions of GTs | ||
650 | 4 | |a Journal Article | |
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700 | 1 | |a Utkina, Natalia |e verfasserin |4 aut | |
700 | 1 | |a Danilov, Leonid |e verfasserin |4 aut | |
700 | 1 | |a Zhou, Dawei |e verfasserin |4 aut | |
700 | 1 | |a Torgov, Vladimir |e verfasserin |4 aut | |
700 | 1 | |a Veselovsky, Vladimir |e verfasserin |4 aut | |
700 | 1 | |a Liu, Bin |e verfasserin |4 aut | |
700 | 1 | |a Feng, Lu |e verfasserin |4 aut | |
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