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

Microbial Bioremediation of Plastics01:28

Microbial Bioremediation of Plastics

Polyethylene terephthalate (PET) is a synthetic polymer widely utilized in the packaging industry, particularly for bottles and containers. Due to its chemical stability and durability, PET accumulates in the environment, contributing significantly to plastic pollution. It comprises repeating units of terephthalic acid and ethylene glycol, resulting in a semi-crystalline structure that is resistant to natural degradation processes.A notable breakthrough in plastic biodegradation came with the...
Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

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 biosynthesis begins in...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Biosynthesis in Bacteria01:24

Biosynthesis in Bacteria

Biosynthesis in bacteria is a fundamental anabolic process that generates essential macromolecules, including proteins, nucleic acids, lipids, and polysaccharides. These macromolecules are critical for cellular growth, replication, and function. The process is tightly regulated and energetically linked to catabolic pathways to ensure optimal resource utilization.Biosynthetic pathways begin with precursor metabolites such as pyruvate, acetyl-CoA, and glucose-6-phosphate derived from glycolysis,...

You might also read

Related Articles

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

Sort by
Same author

Butuanimides, Fatty Acid Synthesis-Inhibiting Antibiotics from Symbiotic Bacteria.

ACS chemical biology·2026
Same author

Detection of unusually high transcriptomic and proteomic abundance of bromoform-synthesizing halogenase in marine macroalgae <i>Asparagopsis taxiformis</i>.

Frontiers in Marine Science·2026
Same author

Differential membrane lipid disruption by lipopeptide antibiotics, colistin and turnercyclamycins.

Nature communications·2026
Same author

An Alkaloid Biosynthetic Gene Bundle in Animals.

Journal of the American Chemical Society·2026
Same author

Artificial Multidomain Ribosomally Synthesized and Post-translationally Modified Peptide Enzymes for Farnesylated Peptide Library Generation.

ACS synthetic biology·2025
Same author

Alkali Cation- and Borate-Binding States of Tartrolon Antibiotics.

Journal of natural products·2025
Same journal

The Hedgehog Pathway Effector Smoothened Exhibits Signaling Competency in the Absence of Ciliary Accumulation.

Chemistry & biology·2017
Same journal

DIVERSE System: De Novo Creation of Peptide Tags for Non-enzymatic Covalent Labeling by In Vitro Evolution for Protein Imaging Inside Living Cells.

Chemistry & biology·2015
Same journal

Differential Regulation of Specific Sphingolipids in Colon Cancer Cells during Staurosporine-Induced Apoptosis.

Chemistry & biology·2015
Same journal

Synthetic Peptides as cGMP-Independent Activators of cGMP-Dependent Protein Kinase Iα.

Chemistry & biology·2015
Same journal

Unraveling the B. pseudomallei Heptokinase WcbL: From Structure to Drug Discovery.

Chemistry & biology·2015
Same journal

Vitamin C as Cancer Destroyer, Investigating Sulfhydration, and the Variability in CFTR Interactome.

Chemistry & biology·2015
See all related articles

Related Experiment Video

Updated: May 23, 2026

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes T&#252;6028
09:08

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028

Published on: January 13, 2017

Cleaning up polyketide synthases.

Jason C Kwan1, Eric W Schmidt

  • 1Department of Medicinal Chemistry, University of Utah, Salt Lake City, UT 84112, USA.

Chemistry & Biology
|March 27, 2012
PubMed
Summary
This summary is machine-generated.

Complex enzymes called polyketide synthases sometimes err. A new study reveals acyltransferases correct these mistakes by removing key intermediates, aiding polyketide biosynthesis research.

More Related Videos

A Purification and In Vitro Activity Assay for a (p)ppGpp Synthetase from Clostridium difficile
09:53

A Purification and In Vitro Activity Assay for a (p)ppGpp Synthetase from Clostridium difficile

Published on: November 3, 2018

Looking Outwards: Isolation of Cyanobacterial Released Carbohydrate Polymers and Proteins
06:58

Looking Outwards: Isolation of Cyanobacterial Released Carbohydrate Polymers and Proteins

Published on: May 27, 2019

Related Experiment Videos

Last Updated: May 23, 2026

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes T&#252;6028
09:08

From a Natural Product to Its Biosynthetic Gene Cluster: A Demonstration Using Polyketomycin from Streptomyces diastatochromogenes Tü6028

Published on: January 13, 2017

A Purification and In Vitro Activity Assay for a (p)ppGpp Synthetase from Clostridium difficile
09:53

A Purification and In Vitro Activity Assay for a (p)ppGpp Synthetase from Clostridium difficile

Published on: November 3, 2018

Looking Outwards: Isolation of Cyanobacterial Released Carbohydrate Polymers and Proteins
06:58

Looking Outwards: Isolation of Cyanobacterial Released Carbohydrate Polymers and Proteins

Published on: May 27, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Polyketide synthases (PKS) are complex multi-enzyme systems responsible for producing a vast array of natural products.
  • These intricate biosynthetic pathways are prone to errors, potentially leading to non-functional or undesired products.
  • Understanding error-correction mechanisms is crucial for optimizing PKS function and product yield.

Purpose of the Study:

  • To identify the specific enzymes responsible for correcting errors in polyketide biosynthesis.
  • To elucidate the mechanism by which these error-correcting enzymes function.
  • To explore the potential applications of this error-correction activity in synthetic biology and natural product discovery.

Main Methods:

  • Biochemical assays to test the hydrolytic activity of various enzymes on PKS intermediates.
  • Enzyme purification and characterization.
  • Analysis of PKS products in the presence and absence of the identified error-correcting enzymes.

Main Results:

  • A discrete family of acyltransferases was identified as responsible for hydrolyzing key biosynthetic intermediates.
  • These acyltransferases act as an error-correction mechanism within the PKS multi-enzyme complex.
  • The identified enzymes effectively remove aberrant intermediates, improving the fidelity of polyketide synthesis.

Conclusions:

  • Acyltransferases play a critical role in ensuring the accuracy of polyketide biosynthesis.
  • This error-correction system is essential for producing functional polyketide natural products.
  • The discovered acyltransferase activity offers potential for engineering PKS pathways and tailoring small molecule synthesis, particularly for uncultivated organisms.