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

Relaxed specificity in aromatic prenyltransferases.

Patrice Koehl

    Nature Chemical Biology
    |January 13, 2006
    PubMed
    Summary

    Aromatic prenyltransferase enzymes can process various aromatic polyketides. This study reveals their mechanism for controlling prenyl side chain length during natural product biosynthesis.

    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

    Realistic transition paths for large biomolecular systems: A Langevin bridge approach.

    The Journal of chemical physics·2026
    Same author

    Persistence diagrams as morphological signatures of cells: A method to measure and compare cells within a population.

    PLoS computational biology·2026
    Same author

    Physicist's view on the unbalanced k-cardinality assignment problem.

    Physical review. E·2024
    Same author

    MinActionPath2: path generation between different conformations of large macromolecular assemblies by action minimization.

    Nucleic acids research·2024
    Same author

    Analyzing the Geometry and Dynamics of Viral Structures: A Review of Computational Approaches Based on Alpha Shape Theory, Normal Mode Analysis, and Poisson-Boltzmann Theories.

    Viruses·2023
    Same author

    Computing the Volume, Surface Area, Mean, and Gaussian Curvatures of Molecules and Their Derivatives.

    Journal of chemical information and modeling·2023

    Area of Science:

    • Biochemistry
    • Natural Product Biosynthesis

    Background:

    • Prenylation is a key enzymatic reaction in the formation of numerous natural products.
    • Aromatic prenyltransferases are crucial enzymes that catalyze the attachment of prenyl groups to aromatic substrates.

    Discussion:

    • This research elucidates the structural and mechanistic basis for aromatic prenyltransferase substrate promiscuity.
    • The findings highlight how these enzymes accommodate diverse aromatic polyketides while maintaining regioselectivity and controlling prenyl chain length.

    Key Insights:

    • Aromatic prenyltransferases exhibit remarkable tolerance for a wide range of aromatic polyketide substrates.
    • Enzyme active site flexibility and specific amino acid residues are critical for accommodating diverse substrates.
    • Precise control over prenyl chain length is achieved through a combination of steric and electronic factors within the enzyme's active site.

    Outlook:

    • Understanding these enzymatic mechanisms can aid in the rational design of novel prenylated compounds.
    • This knowledge could facilitate the engineering of prenyltransferases for synthetic biology applications and drug discovery.
    • Further studies could explore the evolutionary adaptations of prenyltransferases in different natural product pathways.

    Related Experiment Videos