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

Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

6.8K
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...
6.8K
ATP Synthase: Structure01:18

ATP Synthase: Structure

16.6K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
16.6K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

18.1K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
18.1K
Biosynthesis of Nucleic Acids01:28

Biosynthesis of Nucleic Acids

1.4K
Nucleic acid biosynthesis is a fundamental biochemical process that produces the purine and pyrimidine nucleotides essential for DNA and RNA synthesis. This pathway maintains a balanced nucleotide pool, preventing imbalances that could jeopardize genetic integrity and cellular function. Given the crucial role of nucleotides, their synthesis is tightly regulated to ensure proper cellular homeostasis.Purine BiosynthesisThe biosynthesis of purine nucleotides begins with ribose-5-phosphate, a...
1.4K
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

5.3K
The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
 
Most enzymes...
5.3K
Preparation of Diols and Pinacol Rearrangement01:57

Preparation of Diols and Pinacol Rearrangement

4.3K
Compounds bearing two hydroxyl groups are known as diols. When the hydroxyl groups are located on adjacent carbon atoms, the diols are called vicinal diols or glycols. Under acidic conditions, vicinal diols undergo a specific reaction called pinacol rearrangement.
The reaction begins with transferring a proton from the acid catalyst to one of the hydroxyl groups, producing an oxonium ion.
4.3K

You might also read

Related Articles

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

Sort by
Same author

Analytical Ultracentrifugation in Aotearoa: A Brief History of the Technique and its Place Among Other Tools Used to Investigate Biomolecular Interactions.

Journal of the Royal Society of New Zealand·2026
Same author

ZNRF3 and RNF43 are active monomeric E3 ubiquitin ligases that self-associate.

Science signaling·2026
Same author

Whole genome sequencing of three cloacal bacterial isolates from migratory birds.

Microbiology resource announcements·2026
Same author

Whole-genome sequencing and annotation of six metallotolerant bacterial isolates recovered from a retention pond at the Rochester Institute of Technology, New York.

Microbiology resource announcements·2026
Same author

Comprehensive cross-cohort analysis reveals global gut microbiome signatures of celiac disease.

Communications medicine·2026
Same author

Whole-genome sequencing of two endophytic bacteria from immature cones of Northern white cedar (<i>Thuja occidentalis</i>).

Microbiology resource announcements·2026

Related Experiment Video

Updated: Mar 6, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.4K

Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and Evolution.

F Grant Pearce1, André O Hudson2, Kerry Loomes3

  • 1Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Private Bag 4800, Christchurch, 8041, New Zealand.

Sub-Cellular Biochemistry
|March 9, 2017
PubMed
Summary
This summary is machine-generated.

Dihydrodipicolinate synthase, key in lysine biosynthesis, shows diverse quaternary structures across species, impacting its function and regulation. A human enzyme discovery raises concerns for drug development targeting bacterial forms.

Keywords:
4-Hydroxy-2-oxoglutarate aldolaseDihydrodipicolinate synthaseLysine biosynthesis

More Related Videos

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
10:39

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

31.1K
Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
08:31

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

Published on: October 3, 2018

9.0K

Related Experiment Videos

Last Updated: Mar 6, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.4K
Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
10:39

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

31.1K
Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
08:31

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

Published on: October 3, 2018

9.0K

Area of Science:

  • Biochemistry
  • Enzymology
  • Evolutionary Biology

Background:

  • Lysine biosynthesis is essential in plants, bacteria, archaea, and fungi, but not mammals.
  • Dihydrodipicolinate synthase (DDPS) catalyzes the first committed step in this pathway.
  • Bacterial lysine biosynthesis involves four distinct pathways from tetrahydrodipicolinate to meso-diaminopimelate.

Purpose of the Study:

  • To review the structure, function, and evolutionary aspects of dihydrodipicolinate synthase (DDPS).
  • To examine the variability in DDPS quaternary structure across different species.
  • To discuss the implications of a newly discovered human DDPS-like enzyme for drug development.

Main Methods:

  • Structural characterization of DDPS from various bacterial and plant species.
  • Analysis of enzyme oligomeric states and their role in catalysis and regulation.
  • Review of existing literature on DDPS evolution and related human enzymes.

Main Results:

  • DDPS exhibits significant quaternary structure variability, suggesting evolutionary divergence.
  • The oligomeric state of DDPS is crucial for both catalytic activity and allosteric regulation by lysine.
  • A human enzyme, 4-hydroxy-2-oxoglutarate aldolase, shares homology with bacterial DDPS.

Conclusions:

  • The diverse quaternary structures of DDPS reflect its evolutionary adaptation.
  • Understanding DDPS structure-function relationships is key to its regulation.
  • The existence of a human DDPS-like enzyme necessitates careful consideration in developing drugs targeting bacterial DDPS to avoid mammalian toxicity.