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Chen C, Liu B, Xu Y, Utkina N, Zhou D, Danilov L, Torgov V, Veselovsky V, Feng L
Biochemical characterization of the novel a-1,3-galactosyltransferase WclR from Escherichia coli O3
Carbohydrate Research 430 (2016)
36-43
|
b-L-RhapNAc-(1-4)-+ a-D-Glcp-(1-4)-+
| |
-3)-b-D-GlcpNAc-(1-3)-a-D-Galp-(1-3)-b-D-GlcpNAc-(1- |
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Escherichia coli O3
(NCBI TaxID 2234097,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 27196310Publication DOI: 10.1016/j.carres.2016.04.012Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: fenglu63
nankai.edu.cn
Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, TEDA School of Biological Sciences and Biotechnology, Nankai University, Tianjin, China, The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, Tianjin, China
Glycosyltransferases (GTs) catalyze the formation of regio- and stereo-specific glycosidic linkages between specific sugar donors and recipients. In this study, the function of the gene wclR from the Escherichia coli O3 O-antigen gene cluster that encodes an ? 1, 3-galactosyltransferase (GalT) that acts on the linkage Gal α1,3-GlcNAc was biochemically characterized. WclR 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-MS(n)) and galactosidase digestion, using UDP-Gal as the donor substrate and the synthetic acceptor substrate GlcNAc-PP-De (decyl diphosphate N-acetylglucosamine). The physiochemical properties and the substrate specificity of WclR were investigated. WclR is the first bacterial GalT characterized that acts on the linkage Gal α1,3-GlcNAc. This study enhanced our knowledge of the diversified functions of GTs and provided a novel enzyme source for possible pharmaceutical application.
Escherichia coli, mass spectrometry, galactosyltransferase, O-antigen gene cluster, WclR
Structure type: suggested polymer biological repeating unit
Location inside paper: p.37, fig.1
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_135813,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_983931,SB_173,SB_192,SB_7
Methods: PCR, Western blotting, genetic methods, biochemical methods, enzyme assay, LC-ESI-MS, CID-ESI-IT-MS
Comments, role: biological repeat frame was based on [PMID:27196310]
Related record ID(s): 10304, 20634, 22724
NCBI Taxonomy refs (TaxIDs): 2234097Reference(s) to other database(s): GTC:G44739ZN, GlycomeDB:
28095
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Chen C, Hou X, Utkina N, Danilov L, Zhou D, Torgov V, Veselovsky V, Liu B, Feng L
Identification and biochemical characterization of a novel a-1,3-mannosyltransferase WfcD from Escherichia coli O141
Carbohydrate Research (2017)
78-86
|
b-D-GlcpA-(1-2)-+
|
-4)-a-D-Manp-(1-3)-a-D-Manp6Ac-(1-3)-b-D-GlcpNAc-(1-
|
a-L-Rhap-(1-3)-+ |
Show graphically |
Escherichia coli O141
(Ancestor NCBI TaxID 562,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 ]
NCBI PubMed ID: 28402841Publication DOI: 10.1016/j.carres.2017.04.003Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: fenglu63
nankai.edu.cn
Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin, China, The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, 23 Hongda Street, TEDA, Tianjin, China
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.
Escherichia coli, mass spectrometry, Mannosyltransferase, WfcD
Structure type: polymer chemical repeating unit
Location inside paper: p.79, fig.1
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_115136,IEDB_130701,IEDB_135813,IEDB_136105,IEDB_137340,IEDB_140630,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_225177,IEDB_423153,IEDB_885823,IEDB_983930,SB_197,SB_44,SB_67,SB_72
Methods: SDS-PAGE, ESI-MS/MS, MALDI-MS, biochemical methods, enzyme assay, LC-MS, CID-ESI-IT-MS, kinetics assay
Related record ID(s): 12067
NCBI Taxonomy refs (TaxIDs): 562Reference(s) to other database(s): GTC:G84496XY
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Chen C, Hou X, Utkina N, Danilov L, Zhou D, Torgov V, Veselovsky V, Liu B, Feng L
Identification and biochemical characterization of a novel a-1,3-mannosyltransferase WfcD from Escherichia coli O141
Carbohydrate Research (2017)
78-86
Escherichia coli O141
(Ancestor NCBI TaxID 562,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 ]
The structure was elucidated in this paperNCBI PubMed ID: 28402841Publication DOI: 10.1016/j.carres.2017.04.003Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: fenglu63
nankai.edu.cn
Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin, China, The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, 23 Hongda Street, TEDA, Tianjin, China
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.
Escherichia coli, mass spectrometry, Mannosyltransferase, WfcD
Structure type: oligomer
Location inside paper: abstract, fig.3
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130701,IEDB_141807,IEDB_144983,IEDB_150077,IEDB_151531,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72
Methods: SDS-PAGE, ESI-MS/MS, MALDI-MS, biochemical methods, enzyme assay, LC-MS, CID-ESI-IT-MS, kinetics assay
Enzymes that release or process the structure: WfcD (a-1,3-mannosyltransferase)
Synthetic data: enzymatic
Related record ID(s): 11880
NCBI Taxonomy refs (TaxIDs): 562
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There is only one chemically distinct structure:
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