Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
];
infection due to Salmonella enterica [ICD11:
XN5VC ]
The structure was elucidated in this paperNCBI PubMed ID: 16276532Publication DOI: 10.1002/bit.20648Journal NLM ID: 7502021Publisher: New York: Wiley-VCH
Correspondence: byungkim
snu.ac.kr
Institutions: School of Chemical and Biological Engineering, Seoul National University, Korea, Interdisciplinary Program for Biochemical Engineering and Biotechnology, Seoul National University, Seoul, 151-742, Korea, Department of Chemical and Biochemical Engineering, Pusan National University, Busan, 609-735, Korea, Institute of Biomolecule Reconstruction, Sunmoon University, Asan, 336-840, Korea
dTDP-L-rhamnose, an important precursor of O-antigen, was prepared on a large scale from dTMP by executing an one-pot reaction in which six enzymes are involved. Two enzymes, dTDP-4-keto-6-deoxy-D-glucose 3,5-epimerase and dTDP-4-keto-rhamnose reductase, responsible for the conversion of dTDP-4-keto-6-deoxy-D-glucose to dTDP-L-rhamnose, were isolated from their putative sequences in the genome of Mesorhizobium loti, functionally expressed in Escherichia coli, and their enzymatic activities were identified. The two enzymes were combined with an enzymatic process for dTDP-4-keto-6-deoxy-D-glucose involving TMP kinase, acetate kinase, dTDP-glucose synthase, and dTDP-glucose 4,6-dehydratase, which allowed us to achieve a preparative scale synthesis of dTDP-L-rhamnose using dTMP and glucose-1-phosphate as starting materials. About 82% yield of dTDP-L-rhamnose was obtained based on initial dTMP concentration at 20 mM dTMP, 1 mM ATP, 10 mM NADH, 60 mM acetyl phosphate, and 80 mM glucose-1-phosphate. From the reaction with 20 ml volume, approximately 180 mg of dTDP-L-rhamnose was obtained in an overall yield of 60% after two-step purification, that is, anion exchange chromatography and gel filtration for desalting. The purified product was identified by HPLC, ESI-MS, and NMR, showing about 95% purity.
dTDP-L-rhamnose, dTDP-4-keto-6-deoxy-D-glucose, dTDP-4-keto-6-deoxy-D-glucose 3, 5-epimerase, dTDP-4-keto-rhamnose reductase
Structure type: monomer
Location inside paper: p.22, fig. 1(3)
Trivial name: dTDP-6-deoxy-D-xylohex-4-ulose, dTDP-4-keto-6-deoxy-α-D-glucose, dTDP-6-dideoxy-xylo-hexos-4-ulose, dTDP-6-deoxy-α-D-xylo-hex-4-ulose, dTDP-4-oxo-6-deoxy-α-D-glucose, dTDP-6-deoxy-D-xylo-hex-4-ulopyranose, dTDP-4-keto-6-deoxy-D-glucose, dTDP-4-keto-6-deoxyglucose
Compound class: nucleoside diphosphate sugar
Contained glycoepitopes: IEDB_138113,IEDB_196259
Methods: 13C NMR, 1H NMR, ESI-MS, NMR-1D, genetic methods
Enzymes that release or process the structure: enzymatic synthesis with four recombinant enzymes
Biosynthesis and genetic data: genetic data, biochemical data
Comments, role: substrate for dTDP-4-keto-6-deoxy-D-glucose 3,5-epimerase and dTDP-4-keto-rhamnose reductase
Related record ID(s): 20190, 20527, 21584, 21690, 23100, 23229, 23326, 24136
NCBI Taxonomy refs (TaxIDs): 1211845,
99287
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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