This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The enzymes involved in converting UDP-GlcA to other UDP-sugars are well described in eukaryotes, but less is known in prokaryotes. Here we identify and characterize a gene (RsU4kpxs) from Ralstonia solanacearum str. GMI1000, which encodes a dual-function enzyme, UDP-4-keto-pentose/UDP-xylose synthase (UXS). One activity is to decarboxylate UDP-glucuronic acid to UDP-?-L-threo-pentopyranosyl-4""""""""-ulose (UDP-4-keto-pentose) in the presence of NAD+. The second converts UDP-4-keto-pentose and NADH to UDP-xylose and NAD+, albeit at a lower rate. The identification of the R. solanacearum enzyme enables us to propose that the ancestral UXS (as well as UDP-apiose synthase or UAXS) diverged into two distinct enzymatic activities in early bacteria. This separation gave rise to the current Uxs in animal, fungus and plant as well as to the plant Uaxs homologs.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR005351-21
Application #
8168895
Study Section
Special Emphasis Panel (ZRG1-IMST-A (40))
Project Start
2010-04-10
Project End
2011-01-31
Budget Start
2010-04-10
Budget End
2011-01-31
Support Year
21
Fiscal Year
2010
Total Cost
$1,685
Indirect Cost
Name
University of Georgia
Department
Type
Organized Research Units
DUNS #
004315578
City
Athens
State
GA
Country
United States
Zip Code
30602
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