Structure activity relationship studies on rhodanines and derived enethiol inhibitors of metallo-β-lactamases

Structure activity relationship studies on rhodanines and derived enethiol inhibitors of metallo-β-lactamases

Metallo-β-lactamases (MBLs) enable bacterial resistance to almost all classes of β-lactam antibiotics. We report studies on enethiol containing MBL inhibitors, which were prepared by rhodanine hydrolysis. The enethiols inhibit MBLs from different subclasses. Crystallographic analyses reveal that the...

Full description

Bibliographic Details
Main Authors:	Zhang, D, Markoulides, MS, Stepanovs, D, Rydzik, AM, El-Hussein, A, Bon, C, Kamps, JJAG, Umland, K-D, Collins, PM, Cahill, ST, Wang, DY, von Delft, F, Brem, J, McDonough, MA, Schofield, CJ
Format:	Journal article
Language:	English
Published:	Elsevier 2018

Similar Items

Rhodanine derived enethiols react to give 1,3-dithiolanes and mixed disulfides †
by: Kamps, JJAG, et al.
Published: (2024)

Rhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibition.
by: Brem, J, et al.
Published: (2014)

Use of ferrous iron by metallo-β-lactamases.
by: Cahill, S, et al.
Published: (2016)

Bicyclic boronate VNRX-5133 inhibits metallo- and serine-β-lactamases
by: Krajnc, A, et al.
Published: (2019)

Structural basis of metallo-β-lactamase inhibition by captopril stereoisomers
by: Brem, J, et al.
Published: (2015)

Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
by: Brem, J, et al.
Published: (2016)

Comparison of verona integron-borne metallo-β-lactamase (VIM) variants reveals differences in stability and inhibition profiles
by: Makena, A, et al.
Published: (2016)

“To cross-seed or not to cross-seed”: A pilot study using metallo-β-lactamases
by: Abuhammad, A, et al.
Published: (2016)

Studies on the Reactions of Biapenem with VIM Metallo β-Lactamases and the Serine β-Lactamase KPC-2
by: Anka Lucic, et al.
Published: (2022-03-01)

Interaction of Avibactam with Class B Metallo-β-Lactamases.
by: Abboud, M, et al.
Published: (2016)

In silico fragment based design identifies subfamily B1 metallo-β-lactamase inhibitors
by: Cain, R, et al.
Published: (2017)

Assay platform for clinically relevant metallo-β-lactamases.
by: van Berkel, S, et al.
Published: (2013)

Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
by: Jürgen Brem, et al.
Published: (2016-08-01)

NMR-filtered virtual screening leads to non-metal chelating metallo-β-lactamase inhibitors
by: Li, G, et al.
Published: (2017)

Monitoring conformational changes in the NDM-1 metallo-β-lactamase by 19F NMR spectroscopy.
by: Rydzik, A, et al.
Published: (2014)

In vitro and in vivo activity of ML302F: a thioenolate inhibitor of VIM-subfamily metallo β-lactamases
by: Betts, J, et al.
Published: (2015)

19F-NMR reveals the role of mobile loops in product and inhibitor binding by the São Paolo metallo-β-lactamase
by: Abboud, M, et al.
Published: (2017)

Monitoring protein-metal binding by 19F NMR – a case study with the New Delhi metallo-β-lactamase 1
by: Mrs ZAHN GOWAR, et al.
Published: (2020)

Faropenem reacts with serine and metallo-β-lactamases to give multiple products
by: Lucic, A, et al.
Published: (2021)

New Delhi metallo-beta-lactamase 1 catalyzes avibactam and aztreonam hydrolysis
by: Lohans, C, et al.
Published: (2017)

New Delhi metallo-β-lactamase-1 catalyses avibactam and aztreonam hydrolysis.
by: Lohans, C, et al.
Published: (2017)

The chemical biology of human metallo-β-lactamase fold proteins.
by: Pettinati, I, et al.
Published: (2016)

Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition
by: Li, G, et al.
Published: (2017)

Structural basis of metallo-β-lactamase inhibition by N-sulfamoylpyrrole-2-carboxylates
by: Farley, AJM, et al.
Published: (2021)

Rh(III)-catalyzed directed C–H carbenoid coupling reveals aromatic bisphosphonates inhibiting metallo- and Serine-β-lactamases
by: Zhang, C, et al.
Published: (2018)

Crystal structures of VIM‐1 complexes explain active site heterogeneity in VIM‐class metallo‐β‐lactamases
by: Salimraj, R, et al.
Published: (2018)

Profiling interactions of vaborbactam with metallo-β-lactamases
by: Langley, G, et al.
Published: (2019)

Cyclobutanone mimics of intermediates in metallo-β-lactamase catalysis.
by: Abboud, M, et al.
Published: (2017)

Optimized synthesis of indole carboxylate metallo-beta-lactamase inhibitor EBL-3183
by: Baran, A, et al.
Published: (2023)

Synthesis of metallo-beta-lactamase inhibitors
by: Walter, M, et al.
Published: (1997)

¹⁹F NMR studies on 𝛾-Butyrobetaine Hydroxylase provide mechanistic insights and suggest a dual inhibition mode
by: Leśniak, RK, et al.
Published: (2019)

Inhibitors of the FEZ-1 metallo-beta-lactamase.
by: Liénard, B, et al.
Published: (2007)

Cyclic Boronates Inhibit All Classes of β-Lactamase.
by: Cahill, S, et al.
Published: (2017)

Metallo-β-lactamase-mediated antimicrobial resistance and progress in inhibitor discovery
by: Yang, Y, et al.
Published: (2023)

Biochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability.
by: Makena, A, et al.
Published: (2014)

Chromophore-linked substrate (CLS405): probing metallo-β-lactamase activity and inhibition.
by: Makena, A, et al.
Published: (2013)

Chromophore-linked substrate (CLS405): Probing metallo-β-lactamase activity and inhibition
by: Makena, A, et al.
Published: (2013)

Metalo-beta-lactamases Metallo-beta-lactamases
by: Rodrigo Elisandro Mendes, et al.
Published: (2006-04-01)

The inhibition of metallo-beta-lactamase by thioxo-cephalosporin derivatives.
by: Tsang, W, et al.
Published: (2004)

Metallo-Beta-Lactamases: NDM
by: Kamil Leis, et al.
Published: (2019-05-01)