Summary of study ST001308

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.

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Study IDST001308
Study Title1H NMR metabolomics corroborates serine hydroxymethyltransferase as the primary target of 2-aminoacrylate in a ridA mutant of Salmonella enterica
Study TypeNMR metabolomics on Salmonella enterica
Study SummaryThe 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
DepartmentMicrobiology, Biochemistry, Complex Carbohydrate Research Center
LaboratoryEdison Lab and Downs lab
Last NameGouveia
First NameGoncalo
Address315 riverbend road, Complex Carbohydrate Research Centre, ATHENS, GA, 30605, USA
Emailgoncalog@uga.edu
Phone7063087500
Submit Date2020-01-22
Num Groups4
Total Subjects40
Raw Data AvailableYes
Raw Data File Type(s).par, pdata, info, .xml
Analysis Type DetailNMR
Release Date2020-03-03
Release Version1
Goncalo Gouveia Goncalo Gouveia
https://dx.doi.org/10.21228/M8S39G
ftp://www.metabolomicsworkbench.org/Studies/ application/zip

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Project:

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
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