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

Chitinolytic enzymes: catalysis, substrate binding, and their application.

T Fukamizo1

  • 1Laboratory of Biophysical Chemistry, Faculty of Agriculture, Kinki University, 3327-204 Nakamachi, Nara 631-8505, Japan. fukamizo@nara.kindai.ac.jp

Current Protein & Peptide Science
|October 9, 2002
PubMed
Summary

Chitinolytic enzymes exhibit diverse catalytic and substrate binding mechanisms distinct from lysozyme. Understanding these mechanisms, particularly for family 18 chitinases, is crucial for their application in agriculture.

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

Site-directed mutagenesis of Asp280 suggests substrate-assisted catalysis of chitinase A1 from Bacillus circulans WL-12.

Journal of bioscience and bioengineering·2005
Same author

Mechanism of chitosanase-oligosaccharide interaction: subsite structure of Streptomyces sp. N174 chitosanase and the role of Asp57 carboxylate.

Journal of biochemistry·2001
Same author

Properties of Manduca sexta chitinase and its C-terminal deletions.

Insect biochemistry and molecular biology·2001
Same author

Binding of a highly de-N-acetylated chitosan to Japanese pheasan lysozyme as measured by 1H-NMR spectroscopy.

Bioscience, biotechnology, and biochemistry·2001
Same author

[A local structure assisting the enzyme catalysis from behind the catalytic center].

Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme·2001
Same author

Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis.

Biochemistry·2001

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Glycosyl hydrolase mechanisms have historically been modeled after lysozyme.
  • Recent studies reveal chitinolytic enzymes possess unique catalytic and substrate binding strategies.
  • Lysozyme's catalytic center features two carboxyl groups, facilitating a single displacement mechanism.

Purpose of the Study:

  • To elucidate the distinct catalytic and substrate binding mechanisms of various chitinolytic enzyme families.
  • To compare these mechanisms with the well-established lysozyme mechanism.
  • To inform the application of chitinolytic enzymes in agriculture.

Main Methods:

  • X-ray crystallography of chitinases and their complexes with substrate analogues.
  • Analysis of catalytic residue positions relative to bound substrate analogues.

Related Experiment Videos

  • Molecular dynamics calculations.
  • Solid-state cross-polarization magic-angle spinning (CP/MAS) nuclear magnetic resonance (NMR) spectroscopy.
  • Main Results:

    • Family 19 chitinases, family 46 chitosanases, and family 23 lysozymes share lysozyme-like catalytic centers and employ a single displacement mechanism.
    • Family 18 chitinases appear to utilize a substrate-assisted mechanism with only one catalytic carboxylate.
    • Differences in binding cleft structures (e.g., (-4) to (+2) for family 18 vs. (-3) to (+3) for others) correlate with functional diversity.

    Conclusions:

    • Chitinolytic enzyme mechanisms vary significantly across different families, diverging from the lysozyme model.
    • The distinct catalytic and binding properties of chitinolytic enzymes are key to their diverse physiological roles.
    • Understanding these mechanisms is vital for optimizing their use in plant protection against fungal pathogens and insect pests.