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pro vyhledávání: '"Timothy K. Richmond"'
Autor:
Alyssa Hetrick, Timothy K. Richmond, David L. Tierney, Hao Yang, Michael W. Crowder, Mahesh Aitha
Publikováno v:
Biochemistry. 51:3839-3847
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
Autor:
Robert M. McCarrick, Michael W. Crowder, Alyssa Hetrick, Zhenxin Hu, Brian Bennett, Althea Gunther, Raquel Reese, Mahesh Aitha, Timothy K. Richmond
The metallo-β-lactamases (MβLs), which require one or two Zn(II) ions in their active sites for activity, hydrolyze the amide bond in β-lactam-containing antibiotics, and render the antibiotics inactive. All known MβLs contain a mobile element ne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3a00ef38115c3e62b300c6a52f83401
https://europepmc.org/articles/PMC4733626/
https://europepmc.org/articles/PMC4733626/
Autor:
Timothy K. Richmond, Dionne H. Griffin, Michael W. Crowder, David L. Tierney, Abraham Jon Moller, Carlo Sanchez, Robert M. Breece, Brian Bennett
Publikováno v:
Biochemistry. 50(42)
In an effort to probe for metal binding to metallo-β-lactamase (MβL) IMP-1, the enzyme was overexpressed, purified, and characterized. The resulting enzyme was shown to bind 2 equiv of Zn(II), exhibit significant catalytic activity, and yield EXAFS