Literature DB >> 35653820

Structural insights into the design of reversible fluorescent probes for metallo-β-lactamases NDM-1, VIM-2, and IMP-1.

Sky Price1, Radhika Mehta1, Dominique Tan1, Abigail Hinojosa1, Pei W Thomas2, Tawanda Cummings1, Walter Fast2, Emily L Que3.   

Abstract

Metallo-β-lactamases (MBLs) are enzymes that are capable of hydrolyzing most β-lactam antibiotics and all clinically relevant carbapenems. We developed a library of reversible fluorescent turn-on probes that are designed to directly bind to the dizinc active site of these enzymes and can be used to study their dynamic metalation state and enzyme-inhibitor interactions. Structure-function relationships with regards to inhibitory strength and fluorescence turn-on response were evaluated for three representative MBLs.
Copyright © 2022. Published by Elsevier Inc.

Entities:  

Keywords:  Antibiotic resistance; Fluorescent probe; Metalloenzyme inhibitor

Mesh:

Substances:

Year:  2022        PMID: 35653820      PMCID: PMC9216179          DOI: 10.1016/j.jinorgbio.2022.111869

Source DB:  PubMed          Journal:  J Inorg Biochem        ISSN: 0162-0134            Impact factor:   4.336


  34 in total

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Authors:  Youngchang Kim; Mark A Cunningham; Joseph Mire; Christine Tesar; James Sacchettini; Andrzej Joachimiak
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9.  Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers.

Authors:  Jürgen Brem; Sander S van Berkel; David Zollman; Sook Y Lee; Opher Gileadi; Peter J McHugh; Timothy R Walsh; Michael A McDonough; Christopher J Schofield
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10.  A Single Salt Bridge in VIM-20 Increases Protein Stability and Antibiotic Resistance under Low-Zinc Conditions.

Authors:  Zishuo Cheng; Ben A Shurina; Christopher R Bethel; Pei W Thomas; Steven H Marshall; Caitlyn A Thomas; Kundi Yang; Robert L Kimble; Jonathan S Montgomery; Matthew G Orischak; Callie M Miller; Jordan L Tennenbaum; Jay C Nix; David L Tierney; Walter Fast; Robert A Bonomo; Richard C Page; Michael W Crowder
Journal:  mBio       Date:  2019-11-19       Impact factor: 7.867

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