Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 19019146Journal NLM ID: 8712028Publisher: Blackwell Publishing
Correspondence: fenglu63
nankai.edu.cn
Institutions: TEDA School of Biological Sciences and Biotechnology, Nankai University, Tianjin, PR China
D-Fucofuranose (D-Fucf) is a component of Escherichia coli O52 O antigen. This uncommon sugar is also the sugar moiety of the anticancer drug - gilvocarcin V produced by many streptomycetes. In E. coli O52, rmlA, rmlB, fcf1 and fcf2 were proposed in a previous study by our group to encode the enzymes of the dTDP-d-Fucf (the nucleotide-activated form of d-Fucf) biosynthetic pathway. In this study, Fcf1 and Fcf2 from E. coli O52 were expressed, purified and assayed for their respective activities. Novel product peaks from enzyme-substrate reactions were detected by capillary electrophoresis and the structures of the product compounds were elucidated by electro-spray ionization mass spectrometry and nuclear magnetic resonance spectroscopy. Fcf1 was confirmed to be a dTDP-6-deoxy-d-xylo-hex-4-ulopyranose reductase for the conversion of dTDP-6-deoxy-d-xylo-hex-4-ulopyranose to dTDP-d-fucopyranose (dTDP-D-Fucp), and Fcf2 a dTDP-d-Fucp mutase for the conversion of dTDP-d-Fucp to dTDP-d-Fucf. The Km of Fcf1 for dTDP-6-deoxy-d-xylo-hex-4-ulopyranose was determined to be 0.38 mM, and of Fcf2 for dTDP-d-Fucp to be 3.43 mM. The functional role of fcf1 and fcf2 in the biosynthesis of E. coli O52 O antigen were confirmed by mutation and complementation tests. This is the first time that the biosynthetic pathway of dTDP-d-Fucf has been fully characterized.
biosynthesis, O antigen, Biosynthetic Pathways, Escherichia coli O52, D-Fucofuranose (D-Fucf)
Structure type: monomer
Location inside paper: p. 1359, fig. 1
Trivial name: dTDP-α-D-glucose, dTDP-α-D-glucopyranose, dTDP-Glc
Contained glycoepitopes: IEDB_138113,IEDB_142488,IEDB_144998,IEDB_145002,IEDB_146664,IEDB_196259,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, sugar analysis, ESI-MS, GLC, genetic methods, HPLC, capillary electrophoresis (CE)
Enzymes that release or process the structure: RmlA, glucose-1-phosphate thymidylyltransferase
Biosynthesis and genetic data: genetic data, biochemical data
Synthetic data: enzymatic
Comments, role: Substrate for biosynthesis of dTDP-D-Fucf.
Related record ID(s): 20190, 21666, 21689, 22754, 23099, 23228, 23326, 23327, 23328, 23792, 23859
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases
There is only one chemically distinct structure:
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