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

Thioester hydrolysis by matrix metalloproteinases

R L Stein1, M Izquierdo-Martin

  • 1Department of Enzymology, Merck Research Laboratories, Rahway, New Jersey 07065.

Archives of Biochemistry and Biophysics
|January 1, 1994
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

Kinetic and mechanistic studies of penicillin-binding protein 2x from Streptococcus pneumoniae.

Biochemistry·2001
Same author

Predisposition to urinary tract epithelial metaplasia in Schistosoma haematobium infection.

The American journal of tropical medicine and hygiene·2001
Same author

Slow-binding inhibition of gamma-glutamyl transpeptidase by gamma-boroGlu.

Biochemistry·2001
Same author

Kinetic and mechanistic studies of signal peptidase I from Escherichia coli.

Biochemistry·2000
Same author

Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids.

Bioorganic & medicinal chemistry letters·1999
Same author

Hearing aid effect in older females.

Journal of the American Academy of Audiology·1998
Same journal

The Binding Affinity and Recognition Specificity of Dopamine to Human Dopamine Receptors can be Rationally Altered by Halogen Doping.

Archives of biochemistry and biophysics·2026
Same journal

Cortical Cholesterol Deficit and Reduced Network Excitability in ApoE-Deficient Mice.

Archives of biochemistry and biophysics·2026
Same journal

Unraveling zinc's impact: Variable effects across concentrations in Phaseolus coccineus thylakoids.

Archives of biochemistry and biophysics·2026
Same journal

Characterizing tumor-associated endothelial cells in clear cell renal cell carcinoma via scRNA-seq and Bulk RNA-seq: construction of a prognostic risk signature.

Archives of biochemistry and biophysics·2026
Same journal

FOSB-Histone deacetylase 6 axis drives hepcidin-mediated ferroptosis in pulmonary ischemia-reperfusion injury.

Archives of biochemistry and biophysics·2026
Same journal

Sevoflurane preconditioning alleviates hypoxia-reoxygenation-induced myocardial injury via regulating the MIR210HG/miR-377-3p/PUM2 axis.

Archives of biochemistry and biophysics·2026
See all related articles

This study investigated peptide hydrolysis by matrix metalloproteinases (MMPs). Both amide and thioester peptides were efficiently hydrolyzed by stromelysin (SLN), collagenase, gelatinase, and thermolysin, revealing broad substrate specificity.

Area of Science:

  • Biochemistry
  • Enzymology
  • Proteolysis

Background:

  • Previous studies suggested specific peptide substrates for stromelysin (SLN).
  • Ac-Pro-Leu-Ala-Nva-TrpNH2 and its thioester derivative were synthesized based on these suggestions.

Purpose of the Study:

  • To investigate the substrate specificity of stromelysin (SLN) and other metalloproteinases.
  • To compare the hydrolysis of amide and thioester peptide bonds by SLN.

Main Methods:

  • Enzyme kinetics assays were performed.
  • Hydrolysis rates (kcat/Km) were measured for various metalloproteinases using synthetic peptide substrates.
  • pH-dependence studies were conducted for SLN-catalyzed hydrolysis.

Main Results:

Related Experiment Videos

  • Both Ac-Pro-Leu-Ala-Nva-TrpNH2 and Ac-Pro-Leu-Ala-SNva-TrpNH2 were efficiently hydrolyzed by SLN, collagenase, gelatinase, and thermolysin.
  • The pH-dependence of the catalytic efficiency (kcat/Km) for SLN-catalyzed thioester hydrolysis mirrored that of amide hydrolysis.
  • No significant mechanistic differences were observed between thioester and amide hydrolysis by SLN.

Conclusions:

  • Matrix metalloproteinases, including SLN, collagenase, and gelatinase, exhibit broad substrate specificity for these synthetic peptides.
  • Thioester and amide bonds are hydrolyzed by SLN via similar mechanisms.
  • These findings contribute to understanding metalloproteinase substrate recognition and catalytic mechanisms.