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

Enzyme Inhibition01:30

Enzyme Inhibition

72.3K
Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
72.3K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

4.8K
Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
4.8K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

4.4K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.4K
Enzymes02:34

Enzymes

68.8K
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
68.8K

You might also read

Related Articles

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

Sort by
Same author

Cryo-EM structure of the human Kir7.1 channel reveals the molecular basis of snowflake vitreoretinal degeneration disease.

Communications biology·2026
Same author

Volatile anaesthetics modulate voltage-gated sodium channel function at a site directly linked to channel gating.

Nature communications·2026
Same author

Assessment of protein incorporation into SBA-15 particles and their structural changes.

European biophysics journal : EBJ·2025
Same author

Adjuvant Effect of Mesoporous Silica SBA-15 of Different Morphologies on Antidiphtheria Immune Response.

ACS omega·2025
Same author

Graphitic Carbon Nitride: Synthesis and Characterization, Monolayer at the Air-Water Interface, Langmuir-Blodgett Films, and Its Photocatalytic Performance.

ACS omega·2025
Same author

Development of Ni-ZnO-ACE-2 peptide hybrids as electrochemical devices for SARS-CoV-2 spike protein detection.

Bioelectrochemistry (Amsterdam, Netherlands)·2025

Related Experiment Video

Updated: Apr 25, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
13:26

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

63.3K

Deconstructing the DGAT1 enzyme: Binding sites and substrate interactions.

José L S Lopes1, Thatyane M Nobre2, Eduardo M Cilli3

  • 1Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, Brazil; Institute of Structural and Molecular Biology, Birkbeck College, University of London, UK.

Biochimica Et Biophysica Acta
|August 26, 2014
PubMed
Summary

Diacylglycerol acyltransferase 1 (DGAT1) enzyme studies reveal two key peptide sites that interact with triacylglyceride synthesis substrates. These findings suggest how DGAT1 catalyzes lipid formation within cellular membranes.

Keywords:
Diacylglycerol acyltransferaseEnzyme catalysisLangmuir monolayerPeptide–lipid interactionSynchrotron radiation circular dichroism (SRCD) spectroscopyTriglyceride synthesis

More Related Videos

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
13:35

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota

Published on: May 23, 2025

1.1K
Modeling an Enzyme Active Site using Molecular Visualization Freeware
14:37

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

11.5K

Related Experiment Videos

Last Updated: Apr 25, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
13:26

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

63.3K
Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
13:35

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota

Published on: May 23, 2025

1.1K
Modeling an Enzyme Active Site using Molecular Visualization Freeware
14:37

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

11.5K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Diacylglycerol acyltransferase 1 (DGAT1) is crucial for triacylglyceride synthesis.
  • Limited structural data exists for DGAT1 despite conserved sequences across organisms.
  • DGAT1 substrate binding sites are predicted in its luminal loop, sharing motifs with ACAT and protein kinases.

Purpose of the Study:

  • To investigate the interaction of DGAT1's predicted substrate binding sites with triacylglyceride synthesis substrates.
  • To elucidate the structural basis of DGAT1's enzymatic activity.

Main Methods:

  • Synchrotron radiation circular dichroism (SRCD) spectroscopy.
  • Fluorescence emission spectroscopy.
  • Adsorption onto lipid monolayers.
  • Analysis of synthetic peptides representing DGAT1 binding sites (Sit1 and Sit2) and an extended peptide.

Main Results:

  • The Sit1 peptide (FYxDWWN motif) showed conformational changes upon substrate binding, indicating acyl chain interaction.
  • The Sit2 peptide (HKWCIRHFYKP motif) interacted with the charged headgroup region of substrates.
  • An extended peptide containing both Sit1 and Sit2 exhibited significant conformational changes, suggesting substrate proximity facilitation.

Conclusions:

  • DGAT1 possesses distinct binding sites for different substrate regions, facilitating triacylglyceride synthesis.
  • The study provides insights into the mechanism of DGAT1 by characterizing substrate-binding site interactions.
  • Structural understanding of DGAT1 can inform future research on lipid metabolism and related diseases.