Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in shigella dysenteriae type 7 and Escherichia coli O7.

Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in shigella dysenteriae type 7 and Escherichia coli O7. Research Abstract Details 

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Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in shigella dysenteriae type 7 and Escherichia coli O7. Abstract Text:

Ying Wang,Yanli Xu,Andrei V Perepelov,Yuanyuan Qi,Yuriy A Knirel,Lei Wang,Lu Feng,Ying Wang,Yanli Xu,Andrei V Perepelov,Yuanyuan Qi,Yuriy A Knirel,Lei Wang,Lu Feng,

O-antigen variation due to the presence of different types of sugars and sugar linkages is important for the survival of bacteria threatened by host immune systems. The O antigens of Shigella dysenteriae type 7 and Escherichia coli O7 contain 4-(N-acetylglycyl)amino-4,6-dideoxy-d-glucose (d-Qui4NGlyAc) and 4-acetamido-4,6-dideoxy-d-glucose (d-Qui4NAc), respectively, which are sugars not often found in studied polysaccharides. In this study, we characterized the biosynthetic pathways for dTDP-d-Qui4N and dTDP-d-Qui4NAc (the nucleotide-activated precursors of d-Qui4NGlyAc and d-Qui4NAc in O antigens). Predicted genes involved in the synthesis of the two sugars were cloned, and the gene products were overexpressed and purified as His-tagged fusion proteins. In vitro enzymatic reactions were carried out using the purified proteins, and the reaction products were analyzed by capillary electrophoresis, electrospray ionization-mass spectrometry, and nuclear magnetic resonance spectroscopy. It is shown that in S. dysenteriae type 7 and E. coli O7, dTDP-d-Qui4N is synthesized from alpha-d-glucose-1-phosphate in three reaction steps catalyzed by glucose-1-phosphate thymidyltransferase (RmlA), dTDP-d-glucose 4,6-dehydratase (RmlB), and dTDP-4-keto-6-deoxy-d-glucose aminotransferase (VioA). An additional acetyltransferase (VioB) catalyzes the conversion of dTDP-d-Qui4N into dTDP-d-Qui4NAc in E. coli O7. Kinetic parameters and some other properties of VioA and VioB are described and differences between VioA proteins from S. dysenteriae type 7 (VioA(D7)) and E. coli O7 (VioA(O7)) discussed. To our knowledge, this is the first time that functions of VioA and VioB have been biochemically characterized. This study provides valuable enzyme sources for the production of dTDP-d-Qui4N and dTDP-d-Qui4NAc, which are potentially useful in the pharmaceutical industry for drug development.

Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in shigella dysenteriae type 7 and Escherichia coli O7. Publishing Authors By Initials

Y Wang,Y Xu,AV Perepelov,Y Qi,YA Knirel,L Wang,L Feng,Y Wang,Y Xu,AV Perepelov,Y Qi,YA Knirel,L Wang,L Feng,

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Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in shigella dysenteriae type 7 and Escherichia coli O7. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of bacteriology

VOLUME: 189

Page Numbers: 8626-35

Journal Abbreviation: J. Bacteriol.

ISSN: 1098-5530

DAY: 28

MONTH: 09

YEAR: 2007

Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in shigella dysenteriae type 7 and Escherichia coli O7. Information

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LANGUAGE: eng

NlmUniqueID: 2985120

Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in shigella dysenteriae type 7 and Escherichia coli O7. Keywords Mesh Terms:

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Grant and Affiliation Information for Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in shigella dysenteriae type 7 and Escherichia coli O7.

AFFILIATION: TEDA School of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin 300457, People's Republic of China. fenglu63@nankai.edu.cn

Country: United States

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MEDLINETA: J Bacteriol

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Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in shigella dysenteriae type 7 and Escherichia coli O7 Related Publications

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