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In E. coli and P. ananatis , 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 + . 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 Enterobacteriaceae family. We found that ydiJ encodes novel D2HGDHs in P. ananatis and E. coli , which were assigned as D2HGDH Pa and D2HGDH Ec , respectively. Inactivation of ydiJ in P. ananatis and E. coli led to the significant accumulation of D-2-HGA. Recombinant D2HGDH Ec and D2HGDH Pa were purified to homogeneity and characterized. D2HGDH Ec and D2HGDH Pa are homotetrameric with a subunit molecular mass of 110 kDa. The pH optimum was 7.5 for D2HGDH Pa and 8.0 for D2HGDH Ec . The Km for D-2-HGA was 208 μM for D2HGDHPa and 83 μM for D2HGDH Ec . The enzymes have strict substrate specificity towards D-2-HGA and displayed maximal activity at 45 °C. Their activity was completely inhibited by 0.5 mM Mn 2+ , Ni 2+ or Co 2+ . The discovery of a novel family of D2HGDHs may provide fundamental information for the metabolic engineering of microbial chassis with desired properties.

Revealing a New Family of D-2-Hydroxyglutarate Dehydrogenases in Escherichia coli and Pantoea ananatis Encoded by ydiJ