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 Concept Videos

Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation01:22

Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation

Glutathione, a tripeptide made up of glutamate, cysteine, and glycine, is a critical player in the detoxification of drugs and xenobiotics via a process known as glutathione conjugation or mercapturic acid formation. This phase II biotransformation reaction involves the covalent binding of glutathione to a drug or its metabolite, enhancing the compound's water solubility and enabling its excretion.
Several distinctive characteristics distinguish glutathione conjugation from other phase II...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

An adaptable, self-organizing, single-cell morphology circuit optimizes suctorian predatory trap structure.

Current biology : CB·2026
Same author

Phosphoproteome-derived peptide libraries for deep specificity profiling of phosphatases and phospholyases.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Phage-assisted continuous evolution of enzymes for noncanonical tyrosine biosynthesis.

bioRxiv : the preprint server for biology·2026
Same author

Enzymatic Bromination of Native Peptides for Late-Stage Structural Diversification via Suzuki-Miyaura Coupling.

ACS chemical biology·2026
Same author

Dynamic UFMylation governs cellular fitness by coordinating multi-organelle proteostasis.

bioRxiv : the preprint server for biology·2026
Same author

Hookworm genes encoding intestinal excreted-secreted proteins are transcriptionally upregulated in response to the host's immune system.

PLoS neglected tropical diseases·2026

Related Experiment Video

Updated: Jun 12, 2026

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
09:14

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Published on: July 20, 2016

MccB-catalyzed C-terminal Thioesterification for Protein Bioconjugation.

Di Yang1, Amy M Weeks1

  • 1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI, USA.

Current Protocols
|June 11, 2026
PubMed
Summary
This summary is machine-generated.

A new enzymatic system using MccB and a TeCH tag enables C-terminal protein thioesterification. This method expands protein bioconjugation strategies, including expressed protein ligation, for biological studies.

Keywords:
expressed protein ligationprotein C terminusprotein bioconjugationprotein thioestersubtiligase

More Related Videos

Synthesis and Bioconjugation of Thiol-Reactive Reagents for the Creation of Site-Selectively Modified Immunoconjugates
08:47

Synthesis and Bioconjugation of Thiol-Reactive Reagents for the Creation of Site-Selectively Modified Immunoconjugates

Published on: March 6, 2019

Related Experiment Videos

Last Updated: Jun 12, 2026

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
09:14

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Published on: July 20, 2016

Synthesis and Bioconjugation of Thiol-Reactive Reagents for the Creation of Site-Selectively Modified Immunoconjugates
08:47

Synthesis and Bioconjugation of Thiol-Reactive Reagents for the Creation of Site-Selectively Modified Immunoconjugates

Published on: March 6, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chemical Biology

Background:

  • Protein bioconjugation is crucial for adding non-encoded functionalities to proteins.
  • C-terminal protein α-thioesters are key intermediates for protein functionalization.
  • Existing methods for thioester synthesis include chemical and intein-mediated approaches.

Purpose of the Study:

  • To outline the application of the MccB/TeCH tag system for protein C-terminal thioesterification.
  • To demonstrate the utility of MccB-generated thioesters in bioconjugation methods.
  • To expand the versatility of protein functionalization techniques.

Main Methods:

  • Utilizing an ATP-driven, MccB-catalyzed enzymatic system for thioester synthesis.
  • Modifying target proteins with a thioesterification C-terminal handle (TeCH tag).
  • Integrating MccB-generated thioesters with expressed protein ligation (EPL) and enzyme-catalyzed EPL.

Main Results:

  • Successful C-terminal thioesterification of proteins using the MccB/TeCH tag system.
  • Demonstrated compatibility of MccB-generated thioesters with EPL and enzyme-catalyzed EPL.
  • Expanded scope and versatility in protein bioconjugation.

Conclusions:

  • The MccB/TeCH tag system provides an efficient enzymatic route for protein C-terminal thioesterification.
  • This system complements existing methods, offering enhanced flexibility for protein functionalization.
  • The generated thioesters are valuable for advanced bioconjugation applications.