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 Experiment Videos

The active centres in penicillin-sensitive enzymes.

J M Ghuysen, J M Frère, M Leyh-Bouille

    Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
    |May 16, 1980
    PubMed
    Summary

    Beta-lactam antibiotics interact with penicillin-sensitive enzymes through a multi-step process involving specific binding sites. This interaction leads to enzyme acylation and regeneration, crucial for antibiotic function.

    Related Concept Videos

    You might also read

    Related Articles

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

    Sort by
    Same author

    Rapid and easy development of versatile tools to study protein/ligand interactions.

    Protein engineering, design & selection : PEDS·2008
    Same author

    Competitive inhibitors of the CphA metallo-beta-lactamase from Aeromonas hydrophila.

    Antimicrobial agents and chemotherapy·2007
    Same author

    Molecular characterisation of a versatile peroxidase from a Bjerkandera strain.

    Journal of biotechnology·2005
    Same author

    A comparison of Bacillus cereus and Aeromonas hydrophilia Zn-beta-lactamases.

    Journal of synchrotron radiation·2004
    Same author

    Role of Cys221 and Asn116 in the zinc-binding sites of the Aeromonas hydrophila metallo-beta-lactamase.

    Cellular and molecular life sciences : CMLS·2003
    Same author

    Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril.

    Journal of molecular biology·2003

    Area of Science:

    • Biochemistry
    • Pharmacology
    • Enzymology

    Background:

    • Beta-lactam antibiotics are critical therapeutics targeting bacterial cell wall synthesis.
    • Penicillin-sensitive enzymes are key players in the mechanism of action of these antibiotics.
    • Understanding the detailed molecular interactions is vital for antibiotic development and overcoming resistance.

    Purpose of the Study:

    • To elucidate the step-by-step molecular interactions between beta-lactam antibiotics and penicillin-sensitive enzymes.
    • To characterize the roles of distinct binding sites and their influence on enzyme activity.
    • To compare the mechanisms of enzyme interaction with beta-lactam antibiotics and peptide substrates.

    Main Methods:

    • Detailed analysis of the multi-step binding and acylation process.

    Related Experiment Videos

  • Identification and characterization of specific binding sites (site 1, 2, and 3) on the enzyme.
  • Investigation of enzyme regeneration pathways and acyl-enzyme complex stability.
  • Comparison of enzyme mechanisms for beta-lactam antibiotics and D-alanyl-D-alanine (D-Ala-D-Ala) peptides.
  • Main Results:

    • Beta-lactam binding involves sequential interactions at binding site 1, followed by site 2, inducing catalytic activity at site 1.
    • Acylation of a serine residue stabilizes the acyl-enzyme complex via interaction with binding site 3.
    • Enzyme regeneration occurs through direct moiety elimination or metabolite splitting.
    • Enzymes exhibit distinct mechanisms for processing beta-lactams and D-Ala-D-Ala peptides, with varying degrees of active site independence.

    Conclusions:

    • The interaction between beta-lactam antibiotics and penicillin-sensitive enzymes is a complex, multi-step process involving precise molecular recognition.
    • Distinct binding sites and their dynamic interplay dictate the enzyme's catalytic activity and substrate processing.
    • Understanding these mechanisms provides insights into antibiotic efficacy and potential resistance strategies.