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

Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

1.1K
Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan...
1.1K
Peptide Bonds02:43

Peptide Bonds

80.1K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
80.1K
Termination of Translation01:44

Termination of Translation

26.5K
The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
26.5K

You might also read

Related Articles

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

Sort by
Same author

High-Throughput Prediction of Protein-Protein Interactions Uncovers Hidden Molecular Networks in Biosynthetic Gene Clusters.

Computational and structural biotechnology journal·2026
Same author

Stigmatellamines A-D: Bacterial Membrane Vesicle-Induced <i>N</i>-Alkylpyridinium Alkaloids from <i>Stigmatella aurantiaca</i>.

Journal of natural products·2026
Same author

A Pseudokinase Catalyzes Nitrile Formation in the Biosynthesis of a Potent Marine Toxin.

Angewandte Chemie (International ed. in English)·2026
Same author

Real-world outcome and dose intensity of Pola-R-CHP versus R-CHOP/R-THP-COP in newly diagnosed diffuse large B-cell lymphoma: a single-center, retrospective cohort study.

BMC cancer·2026
Same author

Gemcitabine, Carboplatin, Dexamethasone, and Rituximab Versus High-Dose Cytarabine-Based Chemotherapy as Second-Line Treatments for Relapsed or Refractory Diffuse Large B-Cell Lymphoma.

Hematological oncology·2025
Same author

An atypical non-ribosomal peptide cyclase catalyzing homochiral coupling with cyclic amine nucleophile.

The Journal of antibiotics·2025

Related Experiment Video

Updated: Nov 13, 2025

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

11.0K

PenA, a penicillin-binding protein-type thioesterase specialized for small peptide cyclization.

Kenichi Matsuda1, Kei Fujita1, Toshiyuki Wakimoto1,2

  • 1Faculty of Pharmaceutical Sciences, Hokkaido University, Kita 12, Nishi 6, Kita-ku, Sapporo 060-0812, Japan.

Journal of Industrial Microbiology & Biotechnology
|March 13, 2021
PubMed
Summary

Penicillin-binding protein-type thioesterases (PBP-type TEs) are novel peptide cyclases. This study shows PenA, a PBP-type TE, specifically cyclizes small peptides, offering insights into enzyme specificity.

Keywords:
BiocatalystCyclaseCyclopeptide

More Related Videos

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 26, 2016

12.1K
Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

2.9K

Related Experiment Videos

Last Updated: Nov 13, 2025

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

11.0K
Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 26, 2016

12.1K
Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

2.9K

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Penicillin-binding protein-type thioesterases (PBP-type TEs) are a class of enzymes catalyzing peptide cyclization.
  • These enzymes are crucial in the biosynthesis of nonribosomal peptides, including cyclic peptides.

Purpose of the Study:

  • To characterize the enzymatic activity and substrate specificity of PenA, a newly identified PBP-type thioesterase.
  • To compare the catalytic behavior of PenA with other known PBP-type thioesterases, such as SurE.
  • To elucidate the structural basis for PenA's substrate specificity.

Main Methods:

  • In vitro enzymatic assays were performed to demonstrate PenA's activity.
  • A series of synthetic substrates were used to analyze PenA's substrate scope.
  • Reaction profiles of PenA and SurE were compared.
  • Computational modeling was employed to investigate structural determinants of substrate specificity.

Main Results:

  • PenA exhibits enzymatic activity in vitro, catalyzing macrolactamization.
  • PenA demonstrates a specialized substrate scope, favoring the cyclization of smaller peptides compared to SurE.
  • Comparative analysis revealed distinct reaction profiles between PenA and SurE.
  • A computational model suggested structural factors contributing to PenA's altered specificity for substrate chain lengths.

Conclusions:

  • PenA is a functional PBP-type thioesterase involved in cyclic peptide biosynthesis.
  • PenA possesses a specialized activity for cyclizing small peptides, distinguishing it from other PBP-type TEs.
  • Structural insights from computational modeling provide a rationale for PenA's substrate specificity, aiding in the understanding of peptide cyclase mechanisms.