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

Active site flexibility in enzyme catalysis

C L Tsou1

  • 1National Laboratory of Biomacromolecules, Academia Sinica, Beijing, China.

Annals of the New York Academy of Sciences
|February 3, 1999
PubMed
Summary
This summary is machine-generated.

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

Tumor necrosis factor-alpha-converting enzyme mediates the inducible cleavage of fractalkine.

The Journal of biological chemistry·2001
Same author

Human placental cytotrophoblasts attract monocytes and CD56(bright) natural killer cells via the actions of monocyte inflammatory protein 1alpha.

The Journal of experimental medicine·2001
Same author

High concentrations of D-glyceraldehyde-3-phosphate dehydrogenase stabilize the enzyme against denaturation by low concentrations of GuHCl.

Biochimica et biophysica acta·2000
Same author

Metal regulation of metallothionein participation in redox reactions.

FEBS letters·2000
Same author

Structure of active site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor.

Journal of molecular biology·1999
Same author

Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies.

Protein science : a publication of the Protein Society·1998
Same journal

Multiomics Profiling During Autoimmune Demyelination Highlights a Complex Regulatory Role for Ataxin-1 in B Cells.

Annals of the New York Academy of Sciences·2026
Same journal

Global Trends in Light Pollution and Their Relationship With Socioeconomic Factors.

Annals of the New York Academy of Sciences·2026
Same journal

Wired for Corruption: Inter-Brain Synchrony Encodes Bribery-Related Value Information and Predicts Bribery Agreement.

Annals of the New York Academy of Sciences·2026
Same journal

LM-YOLO: A Lightweight Multi-Scale Enhanced Model for Forest Smoke Detection Using Unmanned Aerial Vehicles.

Annals of the New York Academy of Sciences·2026
Same journal

Polyrhythm Perception and Production: A Scoping Review.

Annals of the New York Academy of Sciences·2026
Same journal

DARTS-CNN-BiLSTM: Intelligent Fault Diagnosis for Computer Numerical Control Machine Tool Feed System.

Annals of the New York Academy of Sciences·2026
See all related articles

Enzymes rapidly cycle through active site conformations for optimal function. This flexibility, crucial for enzyme activity, is more sensitive to denaturation than the overall molecular structure.

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Enzyme inactivation during denaturation often occurs before global structural changes are detected.
  • This suggests that the enzyme's active site is more flexible and sensitive to denaturation than the entire molecule.
  • The induced fit hypothesis posits enzymes exist in multiple conformational states influenced by ligands.

Purpose of the Study:

  • To explore the relationship between enzyme active site flexibility and catalytic activity.
  • To investigate the role of conformational dynamics in enzyme function and denaturation.

Main Methods:

  • The study discusses theoretical concepts and existing hypotheses regarding enzyme structure and function.
  • It references conventional methods for monitoring molecular conformational changes.

Related Experiment Videos

  • The text implies experimental observations supporting the active site flexibility hypothesis.

    • Main Results:

    • Enzyme active site flexibility is proposed as a key factor preceding global denaturation.
    • A fragile and flexible active site is essential for the full expression of enzyme activity.
    • Rapid interconversion between active site conformations is vital for catalysis.

    Conclusions:

    • The active site's conformational flexibility is critical for enzyme activity.
    • Enzymes likely undergo rapid conformational cycling essential for their catalytic function.
    • Understanding these dynamics offers insights into enzyme stability and function.