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

  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},
  volume={51 18},
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


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