Structural highlights
Function
AMPC_ECOLI This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A small set of boronic acids acting as low nanomolar inhibitors of AmpC beta-lactamase were designed and synthesized in the effort to improve affinity, pharmacokinetic properties, and to provide a valid lead compound. X-ray crystallography revealed the binary complex of the best inhibitor bound to the enzyme, highlighting possibilities for its further rational derivatization and chemical optimization.
Structural study of phenyl boronic acid derivatives as AmpC beta-lactamase inhibitors.,Tondi D, Calo S, Shoichet BK, Costi MP Bioorg Med Chem Lett. 2010 Jun 1;20(11):3416-9. Epub 2010 Apr 9. PMID:20452208[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tondi D, Calo S, Shoichet BK, Costi MP. Structural study of phenyl boronic acid derivatives as AmpC beta-lactamase inhibitors. Bioorg Med Chem Lett. 2010 Jun 1;20(11):3416-9. Epub 2010 Apr 9. PMID:20452208 doi:10.1016/j.bmcl.2010.04.007
