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} }
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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