Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

meta-Directing Deactivators: –NO2, –CN, –CHO, –⁠CO2R, –COR, –CO2H01:13

meta-Directing Deactivators: –NO2, –CN, –CHO, –⁠CO2R, –COR, –CO2H

7.0K
All meta-directing substituents are deactivating groups. These substituents withdraw electrons from the aromatic ring, making the ring less reactive toward electrophilic substitution. For example, the nitration of nitrobenzene is 100,000 times slower than that of benzene because of the deactivating effect of the nitro group. The first step in an electrophilic aromatic substitution is the addition of an electrophile to form a resonance-stabilized carbocation. The energy diagrams for...
7.0K
Adrenergic Agonists: Chemistry and Structure-Activity Relationship01:16

Adrenergic Agonists: Chemistry and Structure-Activity Relationship

4.0K
Adrenergic agonists' structure-activity relationship (SAR) determines their selectivity and efficacy. These agonists comprise a phenylethylamine moiety with an aromatic ring and an ethylamine side chain.
Aromatic ring substitutions: Substituting the aromatic ring with –OH groups at positions 3 and 4 yields catecholamines (e.g., epinephrine), which have a high affinity for adrenoceptors. Hydrogen bonding between –OH groups and receptors enhances adrenergic activity.
Separation of...
4.0K
Nucleophilic Aromatic Substitution: Addition–Elimination (SNAr)01:30

Nucleophilic Aromatic Substitution: Addition–Elimination (SNAr)

5.0K
Nucleophilic substitution in aromatic compounds is feasible in substrates bearing strong electron-withdrawing substituents positioned ortho or para to the leaving group. The reaction proceeds via two steps: the addition of the nucleophile and the elimination of the leaving group.
The reaction begins with an attack of the nucleophile on the carbon that holds the leaving group. This results in the delocalization of the π electrons over the ring carbons. The resonance interaction between...
5.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Active site groove volume may influence the DD-carboxypeptidase activity of <i>E. coli</i> DacD.

Journal of biomolecular structure & dynamics·2026
Same author

The Effectiveness of Digital Therapeutics Intervention in Oral Anticoagulation Management: A Systematic Review and Meta-analysis.

Mayo Clinic proceedings. Digital health·2026
Same author

Attitudes toward patients' safety among healthcare professionals in the United Arab Emirates: A cross-sectional study.

Medicine·2026
Same author

Assessing the association between COVID-19 vaccination and thrombotic thrombocytopenia syndrome (ATTEST Study): Analyses of English data, 2020-2022.

International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases·2025
Same author

Deletion of major shell proteins of ethanolamine utilization microcompartment reduces intrinsic antibiotic resistance, biofilm, and intracellular survival of Salmonella Typhimurium.

Research in microbiology·2025
Same author

Assessment and management of albuminuria in adults.

BMJ (Clinical research ed.)·2025

Related Experiment Video

Updated: Mar 8, 2026

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors
10:29

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Published on: May 9, 2025

2.6K

E152A substitution drastically affects NDM-5 activity.

Gaurav Kumar1, Bagre Issa2, Debasish Kar1

  • 1Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721302, West Bengal, India.

FEMS Microbiology Letters
|January 15, 2017
PubMed
Summary
This summary is machine-generated.

Amino acid substitutions in New Delhi Metallo beta-lactamase-5 (NDM-5) impact its antibiotic resistance. The E152A mutation significantly reduced NDM-5

Keywords:
beta-lactamcarbapenemasemetallo beta-lactamasesthermal stability

More Related Videos

A Scalable, Cell-Based Method for the Functional Assessment of Ube3a Variants
06:35

A Scalable, Cell-Based Method for the Functional Assessment of Ube3a Variants

Published on: October 10, 2022

2.5K
Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
15:05

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

9.4K

Related Experiment Videos

Last Updated: Mar 8, 2026

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors
10:29

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Published on: May 9, 2025

2.6K
A Scalable, Cell-Based Method for the Functional Assessment of Ube3a Variants
06:35

A Scalable, Cell-Based Method for the Functional Assessment of Ube3a Variants

Published on: October 10, 2022

2.5K
Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
15:05

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

9.4K

Area of Science:

  • Microbiology
  • Biochemistry
  • Drug Resistance

Background:

  • New Delhi Metallo beta-lactamase (NDM) is a critical public health threat due to its broad-spectrum hydrolysis of beta-lactam antibiotics, including carbapenems.
  • Amino acid substitutions outside the active site can modulate NDM beta-lactamase activity.

Purpose of the Study:

  • To investigate the impact of amino acid substitutions in the omega-like loop region of NDM-5 on its beta-lactam hydrolyzing activity and antimicrobial resistance.
  • Specifically, to elucidate the role of the E152 residue in NDM-5 function.

Main Methods:

  • Three substitution mutants of NDM-5 (E152A, S191A, D223A) were generated near the active site.
  • Antimicrobial resistance was monitored upon expression of each mutant in a host.
  • Enzyme kinetics (kcat/Km, Km) and thermal stability of wild-type NDM-5 and the E152A mutant were analyzed.

Main Results:

  • The E152A substitution significantly reduced beta-lactam antibiotic resistance compared to wild-type NDM-5.
  • Purified NDM-5 hydrolyzed all tested beta-lactams, while the E152A mutation suppressed this activity.
  • NDM-5 exhibited higher catalytic efficiency (kcat/Km) against penicillins and carbapenems, with lower Km values than NDM-5_E152A.
  • While overall protein folding was unaffected, thermal stability differed between wild-type and mutated NDM-5.

Conclusions:

  • The E152 residue plays a crucial role in regulating the beta-lactam hydrolyzing properties of NDM-5.
  • Targeting specific residues like E152 may offer strategies to combat NDM-mediated antibiotic resistance.