{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T19:06:06Z","timestamp":1792091166623,"version":"4.4.0"},"reference-count":47,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2021,9,22]],"date-time":"2021-09-22T00:00:00Z","timestamp":1632268800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM095837"],"award-info":[{"award-number":["GM095837"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2021,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>YggS is a pyridoxal 5\u2032\u2010phosphate (PLP)\u2010binding protein of the conserved COG0325 family. Despite a connection with vitamin B<jats:sub>6<\/jats:sub> homeostasis in many species, neither a precise biochemical activity nor the molecular mechanism of how YggS contributes to cellular function has been described. In a transposon mutagenesis screen, we found that insertions in <jats:italic>aspC<\/jats:italic> (encoding a PLP\u2010dependent aspartate aminotransferase, EC 2.6.1.1) in a <jats:italic>Salmonella enterica<\/jats:italic> strain lacking <jats:italic>yggS<\/jats:italic> caused a synthetic growth defect, which could be rescued by the addition of exogenous aspartate. Characterization of spontaneous suppressors which improved the growth of the <jats:italic>yggS aspC<\/jats:italic> double mutant suggested that this synthetic aspartate limitation was dependent on TyrB, a PLP\u2010dependent aromatic amino acid aminotransferase (EC 2.6.1.57). Genetic and biochemical data were consistent with the hypothesis that TyrB activity was inhibited by accumulated pyridoxine 5\u2032\u2010phosphate and \u03b1\u2010keto acids caused by a <jats:italic>yggS<\/jats:italic> mutation. This study provides data consistent with a working model implicating YggS in modulating concentrations of B<jats:sub>6<\/jats:sub> vitamers via transamination.<\/jats:p>","DOI":"10.1111\/mmi.14810","type":"journal-article","created":{"date-parts":[[2021,9,9]],"date-time":"2021-09-09T02:14:56Z","timestamp":1631153696000},"page":"1232-1240","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Loss of YggS (COG0325) impacts aspartate metabolism in <i>Salmonella enterica<\/i>"],"prefix":"10.1111","volume":"116","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4380-467X","authenticated-orcid":false,"given":"Huong N.","family":"Vu","sequence":"first","affiliation":[{"name":"Department of Microbiology The University of Georgia Athens Georgia USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1564-6205","authenticated-orcid":false,"given":"Diana 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