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

Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
Enzyme Inhibition01:30

Enzyme Inhibition

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.
Inducible Operons: lac Operon01:25

Inducible Operons: lac Operon

The lac operon in Escherichia coli is a model for understanding inducible gene regulation and metabolic flexibility. It integrates local control by lactose and global regulation through catabolite repression, enabling E. coli to preferentially metabolize glucose when available and switch to lactose utilization when glucose is scarce.Structure and Function of the lac OperonThe lac operon contains three structural genes: lacZ (β-galactosidase), lacY (lactose permease), and lacA (thiogalactoside...

You might also read

Related Articles

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

Sort by
Same author

OptimGS: a dual integrative genomic prediction framework for improving cold stress tolerance in wheat.

Briefings in bioinformatics·2026
Same author

Antioxidant potential and molecular diversity of passion fruit genotypes from Northeast India.

Scientific reports·2026
Same author

Structural and biochemical basis for cannabinoid cyclase activity in marine bacterial flavoenzymes.

Nature chemical biology·2026
Same author

Genomic insights into end-use grain quality and nutritional traits of an ancient Indian dwarf wheat (Triticum sphaerococcum Percival) population using a multi-locus genome-wide association study.

Journal of the science of food and agriculture·2026
Same author

Targeting Biofilm Formation in Acinetobacter baumannii: In Silico Discovery of Novel Candidate Inhibitors for Acyl-Homoserine Lactone Synthase.

Current drug discovery technologies·2026
Same author

Promoting Microbiology Literacy and Holistic Health: IMiLI and IMiLI-SAC Perspectives on Microbes, Diet, Lifestyle and Society-A 5-Year Journey.

Microbial biotechnology·2026

Related Experiment Video

Updated: May 7, 2026

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

Lactoperoxidase: structural insights into the function,ligand binding and inhibition.

Sujata Sharma1, Amit Kumar Singh, Sanket Kaushik

  • 1Department of Biophysics, All India Institute of Medical Sciences New Delhi - 110029, India.

International Journal of Biochemistry and Molecular Biology
|September 20, 2013
PubMed
Summary

Lactoperoxidase (LPO), an enzyme in mammalian secretions, inactivates microbes. Recent structural studies reveal its function and binding mechanisms, highlighting species variations.

Keywords:
Lactoperoxidaseantimicrobiallactoperoxidase systemmammalian heme peroxidasesstructure

More Related Videos

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory
08:02

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory

Published on: August 23, 2018

Measuring Lactase Enzymatic Activity in the Teaching Lab
04:41

Measuring Lactase Enzymatic Activity in the Teaching Lab

Published on: August 6, 2018

Related Experiment Videos

Last Updated: May 7, 2026

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

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory
08:02

Benchtop Immobilized Metal Affinity Chromatography, Reconstitution and Assay of a Polyhistidine Tagged Metalloenzyme for the Undergraduate Laboratory

Published on: August 23, 2018

Measuring Lactase Enzymatic Activity in the Teaching Lab
04:41

Measuring Lactase Enzymatic Activity in the Teaching Lab

Published on: August 6, 2018

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Lactoperoxidase (LPO) is a mammalian heme peroxidase found in exocrine secretions like milk.
  • It plays a crucial role in the innate immune defense by inactivating microorganisms.
  • LPO catalyzes oxidation reactions using hydrogen peroxide.

Purpose of the Study:

  • To review the discovery, structure, function, and applications of Lactoperoxidase (LPO).
  • To analyze species-dependent variations in LPO sequence, structure, and function.
  • To investigate the structural basis of ligand binding, including substrates and inhibitors.

Main Methods:

  • Literature review of LPO research from its discovery to recent structural elucidation.
  • Comparative analysis of LPO sequences and structures across different species.
  • Detailed examination of LPO's catalytic mechanisms and ligand-binding interactions.

Main Results:

  • The three-dimensional crystal structure of LPO has been recently determined, providing new insights.
  • Significant species-dependent variations exist in LPO structure and function.
  • Distinct modes of substrate and inhibitor binding have been identified.

Conclusions:

  • Recent structural insights enhance understanding of LPO's antimicrobial functions.
  • Comparative analyses reveal evolutionary adaptations in LPO across species.
  • Understanding LPO structure-function relationships can inform potential applications.