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

Amino acids03:42

Amino acids

Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
What are Proteins?01:55

What are Proteins?

Overview
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses 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...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...

You might also read

Related Articles

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

Sort by
Same author

Medicago sativa's antixenotic and antibiotic resistance mechanisms differentially impact three members of the Bemisia tabaci species complex.

Scientific reports·2025
Same author

Viral proteins resolve the virus-vector conundrum during hemipteran-mediated transmission by subverting salicylic acid signaling pathway.

Nature communications·2024
Same author

Integrative transcriptomics reveals association of abscisic acid and lignin pathways with cassava whitefly resistance.

BMC plant biology·2023
Same author

Whitefly-Plant Interactions: An Integrated Molecular Perspective.

Annual review of entomology·2023
Same author

Geographical survey of the mycobiome and microbiome of Southern California glassy-winged sharpshooters.

mSphere·2023
Same author

The tomato chloroplast stromal proteome compendium elucidated by leveraging a plastid protein-localization prediction Atlas.

Frontiers in plant science·2023

Related Experiment Video

Updated: Jul 18, 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

Leucine aminopeptidases: diversity in structure and function.

Mikiko Matsui1, Jonathan H Fowler, Linda L Walling

  • 1Department of Botany and Plant Sciences, Center for Plant Cell Biology, University of California, Riverside, CA 92521-0124, USA.

Biological Chemistry
|November 30, 2006
PubMed
Summary

Leucine aminopeptidases (LAPs) are versatile enzymes involved in peptide breakdown. They play crucial roles in mammals, microbes, and plants, from antigen presentation to DNA binding and gene regulation.

More Related Videos

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

An Efficient Method for the Synthesis of Peptoids with Mixed Lysine-type/Arginine-type Monomers and Evaluation of Their Anti-leishmanial Activity
12:02

An Efficient Method for the Synthesis of Peptoids with Mixed Lysine-type/Arginine-type Monomers and Evaluation of Their Anti-leishmanial Activity

Published on: November 2, 2016

Related Experiment Videos

Last Updated: Jul 18, 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

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

An Efficient Method for the Synthesis of Peptoids with Mixed Lysine-type/Arginine-type Monomers and Evaluation of Their Anti-leishmanial Activity
12:02

An Efficient Method for the Synthesis of Peptoids with Mixed Lysine-type/Arginine-type Monomers and Evaluation of Their Anti-leishmanial Activity

Published on: November 2, 2016

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Leucine aminopeptidases (LAPs) are metallopeptidases that remove N-terminal amino acids from peptides.
  • LAPs belong to the M1 or M17 peptidase families, leading to complex nomenclature.
  • These enzymes are essential for cellular maintenance and peptide turnover.

Purpose of the Study:

  • To explore the diverse functions of Leucine aminopeptidases (LAPs) across different biological systems.
  • To highlight the varied roles of M1 and M17 peptidase families.

Main Methods:

  • Literature review of existing research on Leucine aminopeptidases.
  • Comparative analysis of LAP functions in mammals, microbes, and plants.

Main Results:

  • In mammals, LAPs are involved in MHC I antigen presentation, bioactive peptide processing, and vesicle trafficking.
  • Microbial M17 LAPs exhibit proteolysis, DNA binding, transcriptional repression, and recombination.
  • Plant LAPs are implicated in defense, auxin receptor transport, and meiosis.

Conclusions:

  • Leucine aminopeptidases (LAPs) possess a wide range of functions beyond simple peptide hydrolysis.
  • Their roles are critical in diverse biological processes, including immunity, gene regulation, and development.
  • Further research is needed to fully elucidate LAP functions, particularly in plants.