Biochemical and Structural Studies of Uncharacterized Protein PA0743 from Pseudomonas aeruginosa Revealed NAD+-dependent l-Serine Dehydrogenase*

@article{Tchigvintsev2011BiochemicalAS,
  title={Biochemical and Structural Studies of Uncharacterized Protein PA0743 from Pseudomonas aeruginosa Revealed NAD+-dependent l-Serine Dehydrogenase*},
  author={A. Tchigvintsev and A. Singer and G. Brown and Robert L Flick and E. Evdokimova and K. Tan and C. Gonzalez and A. Savchenko and A. Yakunin},
  journal={The Journal of Biological Chemistry},
  year={2011},
  volume={287},
  pages={1874 - 1883}
}
  • A. Tchigvintsev, A. Singer, +6 authors A. Yakunin
  • Published 2011
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • Background: β-Hydroxyacid dehydrogenases are ubiquitous enzymes, most of which remain uncharacterized. Results: Biochemical, crystallographic, and mutational analyses identified uncharacterized Pseudomonas aeruginosa protein PA0743 as a l-serine dehydrogenase and characterized the molecular details of its active site. Conclusion: PA0743 is the first NAD+-dependent l-serine dehydrogenase potentially involved in serine catabolism. Significance: Our study provides molecular insights into the… CONTINUE READING
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