Reference : A minimalistic approach to identify substrate binding features in B1 Metallo-beta-lactam...
Scientific journals : Article
Physical, chemical, mathematical & earth Sciences : Chemistry
http://hdl.handle.net/2268/77943
A minimalistic approach to identify substrate binding features in B1 Metallo-beta-lactamases
English
Poeylaut-Palena, Andres A [> > > >]
Tomatis, Pablo E [> > > >]
Karsisiotis, Andreas I [> > > >]
Damblon, Christian mailto [Université de Liège - ULg > Département de chimie (sciences) > Chimie biologique structurale >]
Mata, Ernesto G [> > > >]
Vila, Alejandro J [> > > >]
2007
Bioorganic & Medicinal Chemistry Letters
Elsevier Science
17
18
5171-5174
Yes (verified by ORBi)
0960-894X
1464-3405
Oxford
United Kingdom
[en] metallo-beta-lactamases ; inhibitor design ; ligand binding ; monocyclic beta-lactams
[en] The 2-oxoazetidinylacetate sodium salt was synthesized as a model of a minimal P-lactam drug. This compound and the monobactam aztreonam were assayed as substrates of the Metallo-p-lactamase Bell. None of them was hydrolyzed by the enzyme. While the azetidinone was not able to bind Bell, aztreonam was shown to bind in a nonproductive mode. These results provide an explanation for the unability of Metallo-beta-lactamases to inactive monobactams and give some clues for inhibitor design. (c) 2007 Elsevier Ltd. All rights reserved.
http://hdl.handle.net/2268/77943
10.1016/j.bmcl.2007.06.089

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