Cargando…

Tebipenem, a New Carbapenem Antibiotic, Is a Slow Substrate That Inhibits the β-Lactamase from Mycobacterium tuberculosis

[Image: see text] The genome of Mycobacterium tuberculosis contains a gene, blaC, which encodes a highly active β-lactamase (BlaC). We have previously shown that BlaC has an extremely broad spectrum of activity against penicillins and cephalosporins but weak activity against newer carbapenems. We ha...

Descripción completa

Detalles Bibliográficos
Autores principales:	Hazra, Saugata, Xu, Hua, Blanchard, John S.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	American Chemical Society 2014
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4053071/ https://www.ncbi.nlm.nih.gov/pubmed/24846409 http://dx.doi.org/10.1021/bi500339j

Ejemplares similares

The in vitro effect of new combinations of carbapenem–β-lactamase inhibitors for Mycobacterium abscessus
por: Fröberg, Gabrielle, et al.
Publicado: (2023)

Structural insight into the inactivation of Mycobacterium tuberculosis non-classical transpeptidase Ldt(Mt2) by biapenem and tebipenem
por: Bianchet, Mario A., et al.
Publicado: (2017)

Variations in the SDN Loop of Class A Beta-Lactamases: A Study of the Molecular Mechanism of BlaC (Mycobacterium tuberculosis) to Alter the Stability and Catalytic Activity Towards Antibiotic Resistance of MBIs
por: Bhattacharya, Sourya, et al.
Publicado: (2021)

1105. Population Pharmacokinetic Analyses for Tebipenem After the Administration of Tebipenem Pivoxil Hydrobromide
por: Ganesan, Harish, et al.
Publicado: (2021)

Crystal structure of tebipenem pivoxil
por: Tang, Chao, et al.
Publicado: (2018)

Population Pharmacokinetic Analyses for Tebipenem after Oral Administration of Pro-Drug Tebipenem Pivoxil Hydrobromide
por: Ganesan, H., et al.
Publicado: (2023)

The Class A β-Lactamase Produced by Burkholderia Species Compromises the Potency of Tebipenem against a Panel of Isolates from the United States
por: Becka, Scott A., et al.
Publicado: (2022)

Phosphate Promotes the Recovery of Mycobacterium tuberculosis β-Lactamase from Clavulanic Acid Inhibition
por: Elings, Wouter, et al.
Publicado: (2017)

Activity of Oral Tebipenem-Avibactam in a Mouse Model of Mycobacterium abscessus Lung Infection
por: Negatu, Dereje A., et al.
Publicado: (2023)

New Conformations of Acylation Adducts of Inhibitors of β-Lactamase from Mycobacterium tuberculosis
por: Tassoni, Raffaella, et al.
Publicado: (2019)

Directed Evolution of Mycobacterium tuberculosis β-Lactamase Reveals Gatekeeper Residue That Regulates Antibiotic Resistance and Catalytic Efficiency
por: Feiler, Christian, et al.
Publicado: (2013)

Atypically Modified Carbapenem Antibiotics Display Improved Antimycobacterial Activity in the Absence of β-Lactamase Inhibitors
por: Gupta, Rashmi, et al.
Publicado: (2021)

Cefdinir and β-Lactamase Inhibitor Independent Efficacy Against Mycobacterium tuberculosis
por: Srivastava, Shashikant, et al.
Publicado: (2021)

Differential Binding of Carbapenems with the AdeABC Efflux Pump and Modulation of the Expression of AdeB Linked to Novel Mutations within Two-Component System AdeRS in Carbapenem-Resistant Acinetobacter baumannii
por: Roy, Subhasree, et al.
Publicado: (2022)

Antibacterial Properties of Tebipenem Pivoxil Tablet, a New Oral Carbapenem Preparation against a Variety of Pathogenic Bacteria in Vitro and in Vivo
por: Yao, Qi, et al.
Publicado: (2016)

KPC-2 β-lactamase enables carbapenem antibiotic resistance through fast deacylation of the covalent intermediate
por: Mehta, Shrenik C., et al.
Publicado: (2020)

In vitro activity of new combinations of β-lactam and β-lactamase inhibitors against the Mycobacterium tuberculosis complex
por: Economou Lundeberg, Elin, et al.
Publicado: (2023)

1038. In Vitro Activity of Tebipenem, an Orally Available Carbapenem Agent, Against a Collection of Surveillance Gram-Positive Clinical Isolates
por: Arends, S J Ryan, et al.
Publicado: (2021)

Mycobacterium tuberculosis β-lactamase variant reduces sensitivity to ampicillin/avibactam in a zebrafish-Mycobacterium marinum model of tuberculosis
por: van Alen, Ilona, et al.
Publicado: (2023)

Erratum: Cefdinir and β-Lactamase Inhibitor Independent Efficacy Against Mycobacterium tuberculosis
Publicado: (2022)

Penicillin Binding Proteins and β-Lactamases of Mycobacterium tuberculosis: Reexamination of the Historical Paradigm
por: Kumar, Gaurav, et al.
Publicado: (2022)

The Effects of One-Point Mutation on the New Delhi Metallo Beta-Lactamase-1 Resistance toward Carbapenem Antibiotics and β-Lactamase Inhibitors: An In Silico Systematic Approach
por: Tran, Van-Thanh, et al.
Publicado: (2022)

Heterogeneity in the M. tuberculosis β-Lactamase Inhibition by Sulbactam
por: Schmidt, Marius, et al.
Publicado: (2023)

Heterogeneity in M. tuberculosis β-lactamase inhibition by Sulbactam
por: Malla, Tek Narsingh, et al.
Publicado: (2023)

Differential active site requirements for NDM-1 β-lactamase hydrolysis of carbapenem versus penicillin and cephalosporin antibiotics
por: Sun, Zhizeng, et al.
Publicado: (2018)

Small Molecule Carboxylates Inhibit Metallo-β-lactamases and Resensitize Carbapenem-Resistant Bacteria to Meropenem
por: Tehrani, Kamaleddin H. M. E., et al.
Publicado: (2020)

Characterization of a Class A β-Lactamase from Francisella tularensis (Ftu-1) Belonging to a Unique Subclass toward Understanding AMR
por: Bhattacharya, Sourya, et al.
Publicado: (2023)

The G132S Mutation Enhances the Resistance of Mycobacterium tuberculosis β-Lactamase against Sulbactam
por: van Alen, Ilona, et al.
Publicado: (2021)

In Vitro Activity of β-Lactams in Combination with β-Lactamase Inhibitors against Mycobacterium tuberculosis Clinical Isolates
por: Li, Fu, et al.
Publicado: (2018)

Cyclodextrins as multifunctional excipients: Influence of inclusion into β-cyclodextrin on physicochemical and biological properties of tebipenem pivoxil
por: Paczkowska, Magdalena, et al.
Publicado: (2019)

Mapping the determinants of catalysis and substrate specificity of the antibiotic resistance enzyme CTX-M β-lactamase
por: Judge, Allison, et al.
Publicado: (2023)

New Delhi Metallo-β-Lactamase-1 in Carbapenem-Resistant Salmonella Strain, China
por: Huang, Jinwei, et al.
Publicado: (2013)

In vitro potency of xeruborbactam in combination with multiple β-lactam antibiotics in comparison with other β-lactam/β-lactamase inhibitor (BLI) combinations against carbapenem-resistant and extended-spectrum β-lactamase-producing Enterobacterales
por: Lomovskaya, Olga, et al.
Publicado: (2023)

Evaluating the Efficacies of Carbapenem/β-Lactamase Inhibitors Against Carbapenem-Resistant Gram-Negative Bacteria in vitro and in vivo
por: El Hafi, Bassam, et al.
Publicado: (2019)

1452. Is Carbapenem-Sparing Therapy as Effective as Carbapenems Against Extended-Spectrum β-Lactamase Producing Enterobacteriaceae in UTI?
por: Hyun, Jonghoon, et al.
Publicado: (2019)

Determining the in vitro susceptibility of tebipenem, an oral carbapenem, against third-generation cephalosporin-resistant Escherichia coli and Klebsiella pneumoniae isolated from bloodstream infections
por: Ranasinghe, Ama, et al.
Publicado: (2022)

484. Metallo-β-Lactamase-Positive Carbapenem-Resistant Enterobacteriaceae and Pseudomonas aeruginosa in the Antibiotic Resistance Laboratory Network, 2017–2018
por: Brown, Allison C, et al.
Publicado: (2019)

Reporting Extended-Spectrum β-Lactamase Positivity May Reduce Carbapenem Overuse
por: Tamma, Pranita D, et al.
Publicado: (2019)

A comprehensive and contemporary “snapshot” of β-lactamases in carbapenem resistant Acinetobacter baumannii
por: Hujer, Andrea M., et al.
Publicado: (2021)

Mechanistic Insights into β-Lactamase-Catalysed Carbapenem Degradation Through Product Characterisation
por: Lohans, Christopher T., et al.
Publicado: (2019)

Cannot write session to /tmp/vufind_sessions/sess_jcrl9bggqqd9rhd5n7rbsr674s