{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10(9)"],"submitter":["Samsonov VV"],"pubmed_abstract":["In <i>E. coli</i> and <i>P. ananatis</i>, L-serine biosynthesis is initiated by the action of D-3-phosphoglycerate dehydrogenase (SerA), which converts D-3-phosphoglycerate into 3-phosphohydroxypyruvate. SerA can concomitantly catalyze the production of D-2-hydroxyglutarate (D-2-HGA) from 2-ketoglutarate by oxidizing NADH to NAD<sup>+</sup>. Several bacterial D-2-hydroxyglutarate dehydrogenases (D2HGDHs) have recently been identified, which convert D-2-HGA back to 2-ketoglutarate. However, knowledge about the enzymes that can metabolize D-2-HGA is lacking in bacteria belonging to the <i>Enterobacteriaceae</i> family. We found that <i>ydiJ</i> encodes novel D2HGDHs in <i>P. ananatis</i> and <i>E. coli</i>, which were assigned as D2HGDH<i>Pa</i> and D2HGDH<i>Ec</i>, respectively. Inactivatio"],"journal":["Microorganisms"],"pagination":["1766"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9504171"],"repository":["biostudies-literature"],"pubmed_title":["Revealing a New Family of D-2-Hydroxyglutarate Dehydrogenases in <i>Escherichia coli</i> and <i>Pantoea ananatis</i> Encoded by <i>ydiJ</i>."],"pmcid":["PMC9504171"],"pubmed_authors":["Rostova JG","Kuznetsova AA","Samsonov VV","Ziyatdinov MK","Samsonova SA","Kiriukhin MY"],"additional_accession":[]},"is_claimable":false,"name":"Revealing a New Family of D-2-Hydroxyglutarate Dehydrogenases in <i>Escherichia coli</i> and <i>Pantoea ananatis</i> Encoded by <i>ydiJ</i>.","description":"In <i>E. coli</i> and <i>P. ananatis</i>, L-serine biosynthesis is initiated by the action of D-3-phosphoglycerate dehydrogenase (SerA), which converts D-3-phosphoglycerate into 3-phosphohydroxypyruvate. SerA can concomitantly catalyze the production of D-2-hydroxyglutarate (D-2-HGA) from 2-ketoglutarate by oxidizing NADH to NAD<sup>+</sup>. Several bacterial D-2-hydroxyglutarate dehydrogenases (D2HGDHs) have recently been identified, which convert D-2-HGA back to 2-ketoglutarate. However, knowledge about the enzymes that can metabolize D-2-HGA is lacking in bacteria belonging to the <i>Enterobacteriaceae</i> family. We found that <i>ydiJ</i> encodes novel D2HGDHs in <i>P. ananatis</i> and <i>E. coli</i>, which were assigned as D2HGDH<i>Pa</i> and D2HGDH<i>Ec</i>, respectively. Inactivatio","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-04-08T10:45:51.097Z","creation":"2024-12-04T01:39:32.861Z"},"accession":"S-EPMC9504171","cross_references":{"pubmed":["36144368"],"doi":["10.3390/microorganisms10091766"]}}