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Related Concept Videos

Peroxisomes01:24

Peroxisomes

Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
Peroxisomes and Mitochondria01:30

Peroxisomes and Mitochondria

Peroxisomes and mitochondria are two important oxygen-utilizing organelles in eukaryotic cells. Mitochondria carry out cellular respiration—the process that converts energy from food into ATP. Peroxisomes carry out a variety of functions, primarily breaking down different substances, such as fatty acids.
The peroxisome is a single membrane-bound cellular organelle that can perform several different functions, including lipid metabolism and chemical detoxification. The enzymes within peroxisomes...
Peroxisomes01:24

Peroxisomes

Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
Autoxidation of Ethers to Peroxides and Hydroperoxides02:23

Autoxidation of Ethers to Peroxides and Hydroperoxides

Ethers represent a class of chemical compounds that become more dangerous with prolonged storage because they tend to form explosive peroxides when standing in the air. Autoxidation is the spontaneous oxidation of a compound in air. In the presence of oxygen, ethers slowly oxidize to form hydroperoxides and dialkyl peroxides.
Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids02:04

Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids

Diols are compounds with two hydroxyl groups. In addition to syn dihydroxylation, diols can also be synthesized through the process of anti dihydroxylation. The process involves treating an alkene with a peroxycarboxylic acid to form an epoxide. Epoxides are highly strained three-membered rings with oxygen and two carbons occupying the corners of an equilateral triangle. This step is followed by ring-opening of the epoxide in the presence of an aqueous acid to give a trans diol.

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Updated: May 18, 2026

Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes
05:57

Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes

Published on: December 19, 2025

Molecular evolution, structure, and function of peroxidasins.

Monika Soudi1, Marcel Zamocky, Christa Jakopitsch

  • 1Department of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology at BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna.

Chemistry & Biodiversity
|September 15, 2012
PubMed
Summary
This summary is machine-generated.

Peroxidasins, a protein subfamily, are crucial for various biological processes including antimicrobial defense and extracellular matrix formation across species. Further research is needed to fully understand their structure and in vivo functions.

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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Molecular Biology

Background:

  • Peroxidasins are subfamily 2 of the peroxidase-cyclooxygenase superfamily, closely related to chordata peroxidases and peroxinectins.
  • These secreted, glycosylated metalloproteins possess a heme peroxidase domain homologous to human lactoperoxidase, alongside immunoglobulin, leucine-rich repeat, and von Willebrand factor C domains.

Purpose of the Study:

  • To reconstruct the phylogeny of the peroxidasin family.
  • To analyze domain assembly variability and catalytic residue occurrence.
  • To critically review existing knowledge on peroxidasin expression, localization, activity, and roles.

Main Methods:

  • Phylogenetic reconstruction of the peroxidasin family.
  • Analysis of domain composition and conserved catalytic residues.
  • Literature review of experimental data on peroxidasins in model organisms.

Main Results:

  • Identified four invertebrate and one vertebrate clade of peroxidasins, including two human representatives.
  • Variability in domain organization across clades was observed.
  • Catalytic residues in the peroxidase domain were analyzed based on mammalian homologues.

Conclusions:

  • Peroxidasins play roles in antimicrobial defense, extracellular matrix formation, and developmental consolidation.
  • Significant research gaps remain, including structural elucidation and in vivo functional studies across diverse organisms.