Proton Nuclear Magnetic Resonance Metabolomics Corroborates Serine Hydroxymethyltransferase as the Primary Target of 2-Aminoacrylate in a <i>ridA</i> Mutant of Salmonella enterica.

Borchert, Andrew J; Gouveia, Goncalo J; Edison, Arthur S; Downs, Diana M

Proton Nuclear Magnetic Resonance Metabolomics Corroborates Serine Hydroxymethyltransferase as the Primary Target of 2-Aminoacrylate in a ridA Mutant of Salmonella enterica.

Borchert, Andrew J; Gouveia, Goncalo J; Edison, Arthur S; Downs, Diana M.

Afiliação

Borchert AJ; Department of Microbiology, University of Georgia, Athens, Georgia, USA.
Gouveia GJ; Department of Biochemistry, University of Georgia, Athens, Georgia, USA.
Edison AS; Department of Biochemistry, University of Georgia, Athens, Georgia, USA.
Downs DM; Department of Genetics, Institute of Bioinformatics, and Complex Carbohydrate Center, University of Georgia, Athens, Georgia, USA.

mSystems ; 5(2)2020 Mar 10.

Article em En | MEDLINE | ID: mdl-32156800

Palavras-chave

1H NMR; 2-aminoacrylate stress; RidA; metabolomics

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2020 Tipo de documento: Article

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2020 Tipo de documento: Article