<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>10(9)</volume><submitter>Samsonov VV</submitter><pubmed_abstract>In &lt;i>E. coli&lt;/i> and &lt;i>P. ananatis&lt;/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&lt;sup>+&lt;/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 &lt;i>Enterobacteriaceae&lt;/i> family. We found that &lt;i>ydiJ&lt;/i> encodes novel D2HGDHs in &lt;i>P. ananatis&lt;/i> and &lt;i>E. coli&lt;/i>, which were assigned as D2HGDH&lt;i>Pa&lt;/i> and D2HGDH&lt;i>Ec&lt;/i>, respectively. Inactivatio</pubmed_abstract><journal>Microorganisms</journal><pagination>1766</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9504171</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Revealing a New Family of D-2-Hydroxyglutarate Dehydrogenases in &lt;i>Escherichia coli&lt;/i> and &lt;i>Pantoea ananatis&lt;/i> Encoded by &lt;i>ydiJ&lt;/i>.</pubmed_title><pmcid>PMC9504171</pmcid><pubmed_authors>Rostova JG</pubmed_authors><pubmed_authors>Kuznetsova AA</pubmed_authors><pubmed_authors>Samsonov VV</pubmed_authors><pubmed_authors>Ziyatdinov MK</pubmed_authors><pubmed_authors>Samsonova SA</pubmed_authors><pubmed_authors>Kiriukhin MY</pubmed_authors></additional><is_claimable>false</is_claimable><name>Revealing a New Family of D-2-Hydroxyglutarate Dehydrogenases in &lt;i>Escherichia coli&lt;/i> and &lt;i>Pantoea ananatis&lt;/i> Encoded by &lt;i>ydiJ&lt;/i>.</name><description>In &lt;i>E. coli&lt;/i> and &lt;i>P. ananatis&lt;/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&lt;sup>+&lt;/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 &lt;i>Enterobacteriaceae&lt;/i> family. We found that &lt;i>ydiJ&lt;/i> encodes novel D2HGDHs in &lt;i>P. ananatis&lt;/i> and &lt;i>E. coli&lt;/i>, which were assigned as D2HGDH&lt;i>Pa&lt;/i> and D2HGDH&lt;i>Ec&lt;/i>, respectively. Inactivatio</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Aug</publication><modification>2026-04-08T10:45:51.097Z</modification><creation>2024-12-04T01:39:32.861Z</creation></dates><accession>S-EPMC9504171</accession><cross_references><pubmed>36144368</pubmed><doi>10.3390/microorganisms10091766</doi></cross_references></HashMap>