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

Erscheinungsjahr:

2017

Erschienen:

2017

Enthalten in:

Zur Gesamtaufnahme - volume:443-444

Enthalten in:

Carbohydrate research - 443-444(2017) vom: 18. Apr., Seite 78-86

Sprache:

Englisch

Beteiligte Personen:

Chen, Chao [VerfasserIn]
Hou, Xi [VerfasserIn]
Utkina, Natalia [VerfasserIn]
Danilov, Leonid [VerfasserIn]
Zhou, Dawei [VerfasserIn]
Torgov, Vladimir [VerfasserIn]
Veselovsky, Vladimir [VerfasserIn]
Liu, Bin [VerfasserIn]
Feng, Lu [VerfasserIn]

Links:

Volltext

Themen:

Detergents
EC 2.4.1.-
Escherichia coli
Journal Article
Mannosyltransferase
Mannosyltransferases
Mass spectrometry
Metals
O Antigens
WfcD

Anmerkungen:

Date Completed 26.12.2017

Date Revised 26.12.2017

published: Print-Electronic

Citation Status MEDLINE

doi:

10.1016/j.carres.2017.04.003

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM270902325