Literature DB >> 17644332

A minimalistic approach to identify substrate binding features in B1 Metallo-beta-lactamases.

Andrés A Poeylaut-Palena1, Pablo E Tomatis, Andreas I Karsisiotis, Christian Damblon, Ernesto G Mata, Alejandro J Vila.   

Abstract

The 2-oxoazetidinylacetate sodium salt was synthesized as a model of a minimal beta-lactam drug. This compound and the monobactam aztreonam were assayed as substrates of the Metallo-beta-lactamase BcII. None of them was hydrolyzed by the enzyme. While the azetidinone was not able to bind BcII, 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.

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Year:  2007        PMID： 17644332     DOI： 10.1016/j.bmcl.2007.06.089

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN： 0960-894X            Impact factor:   2.823


  12 in total

1.  New Delhi Metallo-β-Lactamase 1 Catalyzes Avibactam and Aztreonam Hydrolysis.

Authors:  Christopher T Lohans; Jürgen Brem; Christopher J Schofield
Journal:  Antimicrob Agents Chemother       Date:  2017-11-22       Impact factor: 5.191

2.  Monitoring Ceftazidime-Avibactam and Aztreonam Concentrations in the Treatment of a Bloodstream Infection Caused by a Multidrug-Resistant Enterobacter sp. Carrying Both Klebsiella pneumoniae Carbapenemase-4 and New Delhi Metallo-β-Lactamase-1.

Authors:  Mohamad Yasmin; Derrick E Fouts; Michael R Jacobs; Hanan Haydar; Steven H Marshall; Richard White; Roshan D'Souza; Thomas P Lodise; Daniel D Rhoads; Andrea M Hujer; Laura J Rojas; Claudia Hoyen; Federico Perez; Amy Edwards; Robert A Bonomo
Journal:  Clin Infect Dis       Date:  2020-08-14       Impact factor: 9.079

Review 3.  Carbapenemases in Klebsiella pneumoniae and other Enterobacteriaceae: an evolving crisis of global dimensions.

Authors:  L S Tzouvelekis; A Markogiannakis; M Psichogiou; P T Tassios; G L Daikos
Journal:  Clin Microbiol Rev       Date:  2012-10       Impact factor: 26.132

4.  Bisthiazolidines: A Substrate-Mimicking Scaffold as an Inhibitor of the NDM-1 Carbapenemase.

Authors:  Mariano M González; Magda Kosmopoulou; Maria F Mojica; Valerie Castillo; Philip Hinchliffe; Ilaria Pettinati; Jürgen Brem; Christopher J Schofield; Graciela Mahler; Robert A Bonomo; Leticia I Llarrull; James Spencer; Alejandro J Vila
Journal:  ACS Infect Dis       Date:  2015-07-20       Impact factor: 5.084

Review 5.  New β-Lactamase Inhibitors in the Clinic.

Authors:  Krisztina M Papp-Wallace; Robert A Bonomo
Journal:  Infect Dis Clin North Am       Date:  2016-06       Impact factor: 5.982

Review 6.  New β-lactamase inhibitors: a therapeutic renaissance in an MDR world.

Authors:  Sarah M Drawz; Krisztina M Papp-Wallace; Robert A Bonomo
Journal:  Antimicrob Agents Chemother       Date:  2013-12-30       Impact factor: 5.191

7.  Monitoring conformational changes in the NDM-1 metallo-β-lactamase by 19F NMR spectroscopy.

Authors:  Anna M Rydzik; Jürgen Brem; Sander S van Berkel; Inga Pfeffer; Anne Makena; Timothy D W Claridge; Christopher J Schofield
Journal:  Angew Chem Int Ed Engl       Date:  2014-02-24       Impact factor: 15.336

8.  Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution.

Authors:  María-Rocío Meini; Leticia I Llarrull; Alejandro J Vila
Journal:  Antibiotics (Basel)       Date:  2014-07-01

9.  Complete ¹H, ¹⁵N, and ¹³C resonance assignments of Bacillus cereus metallo-β-lactamase and its complex with the inhibitor R-thiomandelic acid.

Authors:  Andreas Ioannis Karsisiotis; Christian Damblon; Gordon C K Roberts
Journal:  Biomol NMR Assign       Date:  2013-07-10       Impact factor: 0.746

Review 10.  The Chemical Biology of Human Metallo-β-Lactamase Fold Proteins.

Authors:  Ilaria Pettinati; Jürgen Brem; Sook Y Lee; Peter J McHugh; Christopher J Schofield
Journal:  Trends Biochem Sci       Date:  2016-01-21       Impact factor: 13.807
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