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

Molluscan chymotrypsin-like protease: structure, localization, and substrate specificity

J C Groppe1, D E Morse

  • 1Marine Biotechnology Center, University of California, Santa Barbara 93106.

Archives of Biochemistry and Biophysics
|August 15, 1993
PubMed
Summary

Researchers identified a chymotrypsin-like preproprotease in red abalone intestines. This enzyme is highly expressed and appears to activate through an autocatalytic mechanism, differing from typical pancreatic proteases.

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

Cilia from Abalone Larvae Contain a Receptor-Dependent G Protein Transduction System Similar to that in Mammals.

The Biological bulletin·2018
Same author

cDNA Sequences Reveal mRNAs for Two Gα Signal Transducing Proteins from Larval Cilia.

The Biological bulletin·2018
Same author

Enzymatic Characterization of the Morphogen Recognized by Agaricia humilis (Scleractinian Coral) Larvae.

The Biological bulletin·2018
Same author

Specific Inhibitors of Protein Synthesis Do Not Block RNA Synthesis or Settlement in Larvae of a Marine Gastropod Mollusk (Haliotis rufescens).

The Biological bulletin·2018
Same author

Inorganic Overgrowth of Aragonite on Molluscan Nacre Examined by Atomic Force Microscopy.

The Biological bulletin·2017
Same author

Morphogen-Based Chemical Flypaper for Agaricia humilis Coral Larvae.

The Biological bulletin·2017

Area of Science:

  • Biochemistry
  • Marine Biology
  • Enzymology

Background:

  • A novel chymotrypsin-like preproprotease is highly expressed in the distal intestine of the red abalone (Haliotis rufescens).
  • Chymotrypsin-like activity is concentrated in the intestinal lumen, suggesting a digestive role.

Purpose of the Study:

  • To characterize the novel chymotrypsin-like preproprotease from Haliotis rufescens.
  • To elucidate the enzyme's substrate specificity and activation mechanism.

Main Methods:

  • Purification of the enzyme using anion-exchange chromatography.
  • Analysis of tetrapeptide substrates to determine P1 residue specificity.
  • Homology modeling based on conserved amino acid residues in the substrate binding site.

Related Experiment Videos

Main Results:

  • The enzyme was purified to near homogeneity via a single chromatographic step due to high expression and low protein complexity.
  • Protease specificity was confirmed, with optimal cleavage at P1 residues having bulky, gamma-branched side chains.
  • The zymogen activation mechanism appears to be autocatalytic, distinct from the tryptic activation of pancreatic proteases.
  • Sequence analysis predicted unique features, including an unpaired cysteine residue involved in potential thiol-disulfide isomerization.

Conclusions:

  • The red abalone chymotrypsin-like protease exhibits unique substrate specificity and an autocatalytic activation mechanism.
  • The enzyme's distinct properties, including potential conformational isomerism, warrant further investigation into its biological function.