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1. Role of cytosolic, tyrosine‐insensitive prephenate dehydrogenase in Medicago truncatula

   https://doi.org/10.1002/pld3.218  

   Schenck, Craig A.; Westphal, Josh; Jayaraman, Dhileepkumar; Garcia, Kevin; Wen, Jiangqi; Mysore, Kirankumar S.; Ané, Jean‐Michel; Sumner, Lloyd W.; Maeda, Hiroshi A. (May 2020, Plant Direct)

   Abstract l‐Tyrosine (Tyr) is an aromatic amino acid synthesized de novo in plants and microbes downstream of the shikimate pathway. In plants, Tyr and a Tyr pathway intermediate, 4‐hydroxyphenylpyruvate (HPP), are precursors to numerous specialized metabolites, which are crucial for plant and human health. Tyr is synthesized in the plastids by a TyrA family enzyme, arogenate dehydrogenase (ADH/TyrA_a), which is feedback inhibited by Tyr. Additionally, many legumes possess prephenate dehydrogenases (PDH/TyrA_p), which are insensitive to Tyr and localized to the cytosol. Yet the role of PDH enzymes in legumes is currently unknown. This study isolated and characterizedTnt1‐transposon mutants ofMtPDH1(pdh1) inMedicago truncatulato investigate PDH function. The pdh1mutants lackedPDHtranscript and PDH activity, and displayed little aberrant morphological phenotypes under standard growth conditions, providing genetic evidence thatMtPDH1is responsible for the PDH activity detected inM. truncatula. Though plant PDH enzymes and activity have been specifically found in legumes, nodule number and nitrogenase activity ofpdh1 mutants were not significantly reduced compared with wild‐type (Wt) during symbiosis with nitrogen‐fixing bacteria. Although Tyr levels were not significantly different between Wt and mutants under standard conditions, when carbon flux was increased by shikimate precursor feeding, mutants accumulated significantly less Tyr than Wt. These data suggest that MtPDH1 is involved in Tyr biosynthesis when the shikimate pathway is stimulated and possibly linked to unidentified legume‐specific specialized metabolism. 

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2. Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase

   https://doi.org/10.1021/acs.chemrev.1c00914  

   Stripp, Sven T.; Duffus, Benjamin R.; Fourmond, Vincent; Léger, Christophe; Leimkühler, Silke; Hirota, Shun; Hu, Yilin; Jasniewski, Andrew; Ogata, Hideaki; Ribbe, Markus W. (July 2022, Chemical reviews)
3. Promysalin Elicits Species-Selective Inhibition of Pseudomonas aeruginosa by Targeting Succinate Dehydrogenase

   https://doi.org/10.1021/jacs.7b11212  

   Keohane, Colleen E.; Steele, Andrew D.; Fetzer, Christian; Khowsathit, Jittasak; Van Tyne, Daria; Moynié, Lucile; Gilmore, Michael S.; Karanicolas, John; Sieber, Stephan A.; Wuest, William M. (January 2018, Journal of the American Chemical Society)
4. Mammalian dihydropyrimidine dehydrogenase

   https://doi.org/10.1016/j.abb.2021.109066  

   Forouzesh, Dariush C.; Moran, Graham R. (December 2021, Archives of Biochemistry and Biophysics)
5. Structural analysis of wild-type and Val120Thr mutant Candida boidinii formate dehydrogenase by X-ray crystallography

   https://doi.org/10.1107/s2059798323008070  

   Gul, Mehmet; Yuksel, Busra; Bulut, Huri; DeMirci, Hasan (November 2023, Acta Crystallographica Section D Structural Biology)

   Candida boidiniiNAD⁺-dependent formate dehydrogenase (CbFDH) has gained significant attention for its potential application in the production of biofuels and various industrial chemicals from inorganic carbon dioxide. The present study reports the atomic X-ray crystal structures of wild-typeCbFDH at cryogenic and ambient temperatures, as well as that of the Val120Thr mutant at cryogenic temperature, determined at the Turkish Light Source `Turkish DeLight'. The structures reveal new hydrogen bonds between Thr120 and water molecules in the active site of the mutantCbFDH, suggesting increased stability of the active site and more efficient electron transfer during the reaction. Further experimental data is needed to test these hypotheses. Collectively, these findings provide invaluable insights into future protein-engineering efforts that could potentially enhance the efficiency and effectiveness ofCbFDH. 

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