| Literature DB >> 17933532 |
Jennifer K Mitchell1, Desley Pitcher, Bernadette M McArdle, Terese Alnefelt, Sandra Duffy, Vicky Avery, Ronald J Quinn.
Abstract
Fourteen natural products, known to inhibit other proteins of the Zincin-like fold class, were screened for inhibition of the Zincin-like fold metalloprotease thermolysin using mass spectrometry. Fourier Transform Mass Spectrometry was successful in identifying actinonin, a known inhibitor of astacin and stromelysin, to be an inhibitor of thermolysin. Molecular modelling studies have shown that specificity within the Zincin-like fold is determined by Protein Fold Topology.Mesh:
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Year: 2007 PMID: 17933532 DOI: 10.1016/j.bmcl.2007.09.084
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN: 0960-894X Impact factor: 2.823