ArticleBiochemistry2014
Tebipenem, a new carbapenem antibiotic, is a slow substrate that inhibits the β-lactamase from Mycobacterium tuberculosis.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- Resistance of Uropathogens to Tebipenem: An Analysis of the Evidence from In Vitro Antimicrobial Susceptibility Studies.Microorganisms · 2026Review
- Targeting mycobacterial transpeptidases: evaluating the roles of Ldt and PBP inhibition in suppressingAntimicrobial agents and chemotherapy · 2025Article
- Comparative evaluation of five β-Lactamase inhibitors in combination with β-Lactams against multidrug-resistant Mycobacterium tuberculosis in vitro.BMC infectious diseases · 2025Article
- Characterization of a Class A β-Lactamase fromACS bio & med chem Au · 2023Article
- QM/MM Simulations Reveal the Determinants of Carbapenemase Activity in Class A β-Lactamases.ACS infectious diseases · 2022Article
- Are the Newer Carbapenems of Any Value against Tuberculosis.Antibiotics (Basel, Switzerland) · 2022Article
- β-Lactam Antibiotics and β-Lactamase Enzymes Inhibitors, Part 2: Our Limited Resources.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Recommendations to Synthetize Old and New β-Lactamases Inhibitors: A Review to Encourage Further Production.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Variations in the SDN Loop of Class A Beta-Lactamases: A Study of the Molecular Mechanism of BlaC (Frontiers in microbiology · 2021Article
- Structural Basis and Binding Kinetics of Vaborbactam in Class A β-Lactamase Inhibition.Antimicrobial agents and chemotherapy · 2020Article
- Revisiting the β-Lactams for Tuberculosis Therapy with a Compound-Compound Synthetic Lethality Approach.Antimicrobial agents and chemotherapy · 2019Article
- Article
- In Silico Designing of an Industrially Sustainable Carbonic Anhydrase Using Molecular Dynamics Simulation.ACS omega · 2016Article
- New agents for the treatment of drug-resistant Mycobacterium tuberculosis.Advanced drug delivery reviews · 2016Review
- β-Lactam Resistance Mechanisms: Gram-Positive Bacteria and Mycobacterium tuberculosis.Cold Spring Harbor perspectives in medicine · 2016Review
- Carbapenems and Rifampin Exhibit Synergy against Mycobacterium tuberculosis and Mycobacterium abscessus.Antimicrobial agents and chemotherapy · 2015Article
- Kinetic and Structural Characterization of the Interaction of 6-Methylidene Penem 2 with the β-Lactamase from Mycobacterium tuberculosis.Biochemistry · 2015Article
- In vitro susceptibility of Mycobacterium tuberculosis isolates to an oral carbapenem alone or in combination with β-lactamase inhibitors.Antimicrobial agents and chemotherapy · 2014Article
- Oldie but goodie: Repurposing penicillin for tuberculosis.Nature medicine · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
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 have shown that carbapenems such as meropenem, doripenem, and ertapenem react with the enzyme to form enzyme-drug covalent complexes that are hydrolyzed extremely slowly. In the current study, we have determined apparent Km and kcat values of 0.8 μM and 0.03 min(-1), respectively, for tebipenem, a novel carbapenem whose prodrug form, the pivalyl ester, is orally available. Tebipenem exhibits slow tight-binding inhibition at low micromolar concentrations versus the chromogenic substrate nitrocefin. FT-ICR mass spectrometry demonstrated that the tebipenem acyl-enzyme complex remains stable for greater than 90 min and exists as mixture of the covalently bound drug and the bound retro-aldol cleavage product. We have also determined the high-resolution crystal structures of the BlaC-tebipenem covalent acylated adduct (1.9 Å) with wild-type BlaC and the BlaC-tebipenem Michaelis-Menten complex (1.75 Å) with the K73A BlaC variant. These structures are compared to each other and to other carbapenem-BlaC structures.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.