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

Protein Complex Assembly02:41

Protein Complex Assembly

11.3K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
11.3K
Enzymes02:34

Enzymes

82.9K
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...
82.9K
Introduction to Enzymes01:22

Introduction to Enzymes

20.2K
The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that...
20.2K
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

9.0K
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
9.0K
Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

21.0K
Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
21.0K
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

4.2K
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...
4.2K

You might also read

Related Articles

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

Sort by
Same author

Antimicrobial Peptide Fusion and Alginate Encapsulation Broaden the Antibacterial Spectrum and Preserve Storage Stability of the Endolysin <i>Ab</i>Lys1 from <i>Acinetobacter baumannii</i> Phage <i>Ab</i>TZA1.

ACS omega·2026
Same author

A Monocarbonyl Curcuminoid Derivative Inhibits the Activity of Human Glutathione Transferase A4-4 and Chemosensitizes Glioblastoma Cells to Temozolomide.

Pharmaceuticals (Basel, Switzerland)·2024
Same author

Structural Studies of <i>Klebsiella pneumoniae</i> Fosfomycin-Resistance Protein and Its Application for the Development of an Optical Biosensor for Fosfomycin Determination.

International journal of molecular sciences·2024
Same author

Inhibition Analysis and High-Resolution Crystal Structure of <i>Mus musculus</i> Glutathione Transferase P1-1.

Biomolecules·2023
Same author

A Key Role in Catalysis and Enzyme Thermostability of a Conserved Helix H5 Motif of Human Glutathione Transferase A1-1.

International journal of molecular sciences·2023
Same author

Monocarbonyl Curcumin Analogues as Potent Inhibitors against Human Glutathione Transferase P1-1.

Antioxidants (Basel, Switzerland)·2023

Related Experiment Video

Updated: Sep 20, 2025

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.5K

Structural Characterization of Multienzyme Assemblies: An Overview.

Anastassios C Papageorgiou1

  • 1Turku Bioscience Centre, University of Turku and Åbo Akademi University, Turku, Finland. anapap@utu.fi.

Methods in Molecular Biology (Clifton, N.J.)
|June 10, 2022
PubMed
Summary
This summary is machine-generated.

Multienzyme assemblies offer efficient, eco-friendly biocatalysis for industry. Structural insights, particularly from X-ray crystallography, are crucial for understanding and optimizing these complex systems.

Keywords:
BiocatalysisCatalytic mechanismChannelingEnzyme immobilizationEnzyme structureStructure determinationX-ray

More Related Videos

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

6.8K
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

4.0K

Related Experiment Videos

Last Updated: Sep 20, 2025

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.5K
Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

6.8K
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

4.0K

Area of Science:

  • Biocatalysis and Green Chemistry
  • Structural Biology
  • Industrial Biotechnology

Background:

  • Multienzyme assemblies are gaining traction as superior alternatives to single enzymes for industrial applications.
  • They enable cascade reactions, offering advantages like higher yields, faster speeds, and easier separation compared to microbial systems.
  • These assemblies leverage enzyme benefits such as reusability, efficiency, and specificity, aligning with green chemistry principles.

Purpose of the Study:

  • To review the structural characterization of multienzyme assemblies.
  • To highlight the importance of understanding mechanistic details for industrial biotransformation.
  • To showcase examples where structural information elucidates function in these systems.

Main Methods:

  • Review of existing literature on multienzyme assemblies.
  • Focus on structural biology techniques, particularly X-ray crystallography.
  • Analysis of provided examples illustrating structural insights.

Main Results:

  • Structural information is pivotal for characterizing enzymes and their structure-function relationships.
  • X-ray crystallography has been instrumental in revealing mechanistic details of multienzyme assemblies.
  • Detailed characterization is essential for the efficient industrial application of these biocatalysts.

Conclusions:

  • Multienzyme assemblies hold significant potential as biocatalysts in green chemistry and industrial processes.
  • Further detailed structural characterization is necessary to fully exploit their capabilities.
  • X-ray crystallography provides critical insights for the rational design and optimization of multienzyme systems.