Purification and initial biochemical characterization of ATP:Cob(I)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica.

@article{Buan2006PurificationAI,
  title={Purification and initial biochemical characterization of ATP:Cob(I)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica.},
  author={Nicole R. Buan and Jorge C Escalante-Semerena},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 25},
  pages={16971-7}
}
ATP:cob(I)alamin adenosyltransferase (EutT) of Salmonella enterica was overproduced and enriched to approximately 70% homogeneity, and its basic kinetic parameters were determined. Abundant amounts of EutT protein were produced, but all of it remained insoluble. Soluble active EutT protein (approximately 70% homogeneous) was obtained after treatment with detergent. Under conditions in which cobalamin (Cbl) was saturating, Km(ATP) = 10 microm, kcat = 0.03 s(-1), and Vmax = 54.5 nm min(-1… CONTINUE READING
7 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-7 of 7 extracted citations

Similar Papers

Loading similar papers…