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

Solution structure and activity of mouse lysozyme M.

T Obita1, T Ueda, T Imoto

  • 1Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.

Cellular and Molecular Life Sciences : CMLS
|March 5, 2003
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

Social Detachment Influenced Muscle Mass and Strength during the COVID-19 Pandemic in Japanese Community-Dwelling Older Women.

The Journal of frailty & aging·2022
Same author

Life-Long Wheel Running Attenuates Age-Related Fiber Loss in the Plantaris Muscle of Mice: a Pilot Study.

International journal of sports medicine·2016
Same author

Elucidation of the relationship between enzyme activity and internal motion using a lysozyme stabilized by cavity-filling mutations.

Cellular and molecular life sciences : CMLS·2005
Same author

Evidence for a novel racemization process of an asparaginyl residue in mouse lysozyme under physiological conditions.

Cellular and molecular life sciences : CMLS·2005
Same author

Effects of heating procedures on deoxynivalenol, nivalenol and zearalenone levels in naturally contaminated barley and wheat.

Food additives and contaminants·2004
Same author

A small chimerically bifunctional monomeric protein: Tapes japonica lysozyme.

Cellular and molecular life sciences : CMLS·2003

Mouse lysozyme M, a glycoside hydrolase, shares structural similarity with hen lysozyme. Lower hydrolytic activity in mouse lysozyme M is attributed to weaker enzyme-substrate binding and restricted molecular motion.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Lysozymes are glycoside hydrolases crucial in innate immunity.
  • Understanding structural and functional differences between lysozymes is important for biochemical research.

Purpose of the Study:

  • To determine the three-dimensional structure of mouse lysozyme M.
  • To compare the structure and hydrolytic activity of mouse lysozyme M with hen lysozyme.

Main Methods:

  • Heteronuclear NMR spectroscopy was employed to elucidate the 3D structure.
  • Enzyme activity assays were performed using p-nitrophenyl penta N-acetyl-beta-D-chitopentaoside.
  • Binding affinities and internal molecular motions were analyzed.

Main Results:

Related Experiment Videos

  • Mouse lysozyme M possesses four alpha-helices, two 3(10)helices, and anti-parallel beta-sheets, closely resembling hen lysozyme.
  • The pH activity profile of mouse lysozyme M is similar to hen lysozyme, but its overall hydrolytic activity is lower.
  • Analysis revealed a larger dissociation constant for the enzyme-substrate complex and restricted internal motions in mouse lysozyme M.

Conclusions:

  • Mouse lysozyme M exhibits a high degree of structural homology with hen lysozyme.
  • Reduced hydrolytic efficiency of mouse lysozyme M is linked to its enzyme-substrate complex stability and internal dynamics.