Summary of project PR000889
This data is available at the NIH Common Fund's National Metabolomics Data Repository (NMDR) website, the Metabolomics Workbench, https://www.metabolomicsworkbench.org, where it has been assigned Project ID PR000889. The data can be accessed directly via it's Project DOI: 10.21228/M8S39G This work is supported by NIH grant, U2C- DK119886.
See: https://www.metabolomicsworkbench.org/about/howtocite.php
| Project ID: | PR000889 |
| Project DOI: | doi: 10.21228/M8S39G |
| Project Title: | 1H NMR metabolomics confirms serine hydroxymethyltransferase is the primary target of 2-aminoacrylate in a ridA mutant of Salmonella enterica |
| Project Type: | NMR metabolomics Salmonella enterica |
| Project Summary: | The reactive intermediate deaminase RidA (EC: 3.5.99.10) is conserved across all domains of life and deaminates reactive enamine species. When S. enterica ridA mutants are grown in minimal medium, 2-aminoacrylate (2AA) accumulates, damages several pyridoxal 5’-phosphate (PLP)- dependent enzymes, and elicits an observable growth defect. Genetic studies suggested that damage to serine hydroxymethyltransferase (GlyA), and the resultant depletion of 5,10-methelenetetrahydrofolate (5,10-mTHF), was responsible for the observed growth defect. However, the downstream metabolic consequence from GlyA damage by 2AA remains relatively unexplored. This study sought to use untargeted 1H NMR metabolomics to determine whether the metabolic state of a S. enterica ridA mutant was accurately reflected by characterizing growth phenotypes. The data supported the conclusion that metabolic changes in a ridA mutant were due to the IlvA-dependent generation of 2AA, and that the majority of these changes were a consequence of damage to GlyA. While many of the shifts in the metabolome of a ridA mutant could be explained, changes in some metabolites were not easily modeled, suggesting that additional levels of metabolic complexity remain to be unraveled. |
| Institute: | University of Georgia |
| Department: | Microbiology, Biochemistry, Complex Carbohydrate Research Center |
| Laboratory: | Edison Lab and Downs lab |
| Last Name: | Edison |
| First Name: | Arthur |
| Address: | 315 riverbend road, Complex Carbohydrate Research Centre, ATHENS, GA, 30605, USA |
| Email: | aedison@uga.edu |
| Phone: | na |
| Contributors: | Andrew J. Borchert, Goncalo J. Gouveia, Arthur S. Edison, and Diana M. Downs |
Summary of all studies in project PR000889
| Study ID | Study Title | Species | Institute | Analysis(* : Contains Untargted data) | Release Date | Version | Samples | Download(* : Contains raw data) |
|---|---|---|---|---|---|---|---|---|
| ST001308 | 1H NMR metabolomics corroborates serine hydroxymethyltransferase as the primary target of 2-aminoacrylate in a ridA mutant of Salmonella enterica | Salmonella enterica serovar Typhimurium | University of Georgia | NMR | 2020-03-03 | 1 | 120 | Uploaded data (391.1M)* |
