Mechanistic and spectroscopic studies of metallo-β-lactamase NDM-1.

@article{Yang2012MechanisticAS,
  title={Mechanistic and spectroscopic studies of metallo-β-lactamase NDM-1.},
  author={Hao Yang and Mahesh Aitha and Alyssa M Hetrick and Timothy K Richmond and David L Tierney and Michael W Crowder},
  journal={Biochemistry},
  year={2012},
  volume={51 18},
  pages={3839-47}
}
In an effort to biochemically characterize metallo-β-lactamase NDM-1, we cloned, overexpressed, purified, and characterized several maltose binding protein (MBP)-NDM-1 fusion proteins with different N-termini (full-length, Δ6, Δ21, and Δ36). All MBP-NDM-1 fusion proteins were soluble; however, only one, MBP-NDM-1Δ36, exhibited high activity and bound 2 equiv of Zn(II). Thrombin cleavage of this fusion protein resulted in the truncated NDM-1Δ36 variant, which exhibited a k(cat) of 16 s(-1) and a… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 21 extracted citations

Characterization of β-lactamase activity using isothermal titration calorimetry.

Biochimica et biophysica acta. General subjects • 2017
View 1 Excerpt

References

Publications referenced by this paper.
Showing 1-10 of 67 references

Carbapenems: Past, Present, and Future

R A.
Antimicrob. Agents Chemother • 2011
View 5 Excerpts
Highly Influenced

A structural view

C. Yang, Z. Lou, Z. Rao
2011

Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology • 2011

Similar Papers

Loading similar papers…