Optimization of 1, 2, 4-triazole-3-thiones toward broad-spectrum metallo-β-lactamase inhibitors showing potent synergistic activity on VIM-and NDM-1-producing …

A Legru, F Verdirosa, Y Vo-Hoang… - Journal of Medicinal …, 2022 - ACS Publications
Metallo-β-lactamases (MBLs) contribute to the resistance of Gram-negative bacteria to
carbapenems, last-resort antibiotics at hospital, and MBL inhibitors are urgently needed to …

Discovery of 2-aminothiazole-4-carboxylic acids as broad-spectrum metallo-β-lactamase inhibitors by mimicking carbapenem hydrolysate binding

YH Yan, TT Zhang, R Li, SY Wang, LL Wei… - Journal of Medicinal …, 2023 - ACS Publications
Metallo-β-lactamases (MBLs) are zinc-dependent enzymes capable of hydrolyzing all
bicyclic β-lactam antibiotics, posing a great threat to public health. However, there are …

Interactions of hydrolyzed β-lactams with the L1 metallo-β-lactamase: Crystallography supports stereoselective binding of cephem/carbapenem products

P Hinchliffe, K Calvopiña, P Rabe, MF Mojica… - Journal of Biological …, 2023 - ASBMB
L1 is a dizinc subclass B3 metallo-β-lactamase (MBL) that hydrolyzes most β-lactam
antibiotics and is a key resistance determinant in the Gram-negative pathogen …

Are the newer carbapenems of any value against tuberculosis

X Gonzalo, F Drobniewski - Antibiotics, 2022 - mdpi.com
Our aim was to assess whether newer carbapenems with a better administration profile than
meropenem (ertapenem, faropenem and tebipenem) were more effective against …

Time-resolved β-lactam cleavage by L1 metallo-β-lactamase

M Wilamowski, DA Sherrell, Y Kim, A Lavens… - Nature …, 2022 - nature.com
Serial x-ray crystallography can uncover binding events, and subsequent chemical
conversions occurring during enzymatic reaction. Here, we reveal the structure, binding and …

Interplay between the Enamine and Imine Forms of the Hydrolyzed Imipenem in the Active Sites of Metallo-β-lactamases and in Water Solution

AV Krivitskaya, MG Khrenova - Journal of Chemical Information …, 2022 - ACS Publications
Deactivation of the β-lactam antibiotics in the active sites of the β-lactamases is among the
main mechanisms of bacterial antibiotic resistance. As drugs of last resort, carbapenems are …

Small-molecule inhibitors of bacterial-producing metallo-β-lactamases: insights into their resistance mechanisms and biochemical analyses of their activities

YO Ayipo, CF Chong, MN Mordi - RSC Medicinal Chemistry, 2023 - pubs.rsc.org
Antibiotic resistance (AR) remains one of the major threats to the global healthcare system,
which is associated with alarming morbidity and mortality rates. The defence mechanisms of …

The crystal structure of the H116Q mutant of NDM-1: An enzyme devoid of zinc ions

WP Kong, YW Chen, KY Wong - Journal of Structural Biology, 2022 - Elsevier
New Delhi metallo-β-lactamase 1 (NDM-1) is an important causative factor of antimicrobial
resistance due to its efficient hydrolysis of a broad range of β-lactam compounds. The two …

Phenotypic versus molecular assays for detecting carbapenemase-producing Enterobacterales from urinary tract infections

AM Nour El Deen, YS Naga… - Microbes and …, 2024 - journals.ekb.eg
Background: Carbapenem-resistant Enterobacterales (CRE) have been identified as a
public health problem. Treatment options for CRE are limited as they are mostly resistant to …

[PDF][PDF] Time-Resolved β-lactam Cleavage by L1 Metallo-β-Lactamase

A Joachimiak, M Wilamowski, D Sherrell, Y Kim… - 2022 - scholar.archive.org
Time-Resolved β-lactam Cleavage by L1 Metallo-β- Lactamase Page 1 Time-Resolved β-lactam
Cleavage by L1 Metallo-βLactamase Andrzej Joachimiak (  andrzejj@anl.gov ) University …