Proton Nuclear Magnetic Resonance Metabolomics Corroborates Serine Hydroxymethyltransferase as the Primary Target of 2-Aminoacrylate in a <italic toggle="yes">ridA</italic> Mutant of <named-content content-type="genus-species">Salmonella enterica</named-content>

Proton Nuclear Magnetic Resonance Metabolomics Corroborates Serine Hydroxymethyltransferase as the Primary Target of 2-Aminoacrylate in a <italic toggle="yes">ridA</italic> Mutant of <named-content content-type="genus-species">Salmonella enterica</named-content>

ABSTRACT The reactive intermediate deaminase RidA (EC 3.5.99.10) is conserved across all domains of life and deaminates reactive enamine species. When Salmonella enterica ridA mutants are grown in minimal medium, 2-aminoacrylate (2AA) accumulates, damages several pyridoxal 5′-phosphate (PLP)-depende...

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Autores principales: Andrew J. Borchert, Goncalo J. Gouveia, Arthur S. Edison, Diana M. Downs
Formato: article
Lenguaje:EN
Publicado: American Society for Microbiology 2020
Materias:
1H NMR
2-aminoacrylate stress
RidA
metabolomics
Microbiology
QR1-502
Acceso en línea:https://doaj.org/article/40280bad67c446c1aa128e306c7065e7
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