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Related Concept Videos

The Proteasome02:18

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
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The Proteasome01:13

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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Protein Digestion01:02

Protein Digestion

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Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
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The Proteasome Structure01:17

The Proteasome Structure

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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
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A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation
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A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation

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Site-Selective Peptide/Protein Cleavage.

Jizhi Ni1, Motomu Kanai2

  • 1Graduate School of Pharmaceutical Sciences, The University of Tokyo, and JST-ERATO, Kanai Life Science Catalysis Project, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.

Topics in Current Chemistry
|August 8, 2015
PubMed
Summary

Chemical methods enable site-selective peptide and protein degradation, complementing enzymatic approaches. This review covers recent advances in chemical peptide bond cleavage, focusing on mechanisms, reactivity, and substrate scope.

Keywords:
CleavageDegradationPeptide bondsProteinsSite-selectivity

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Area of Science:

  • Chemical Biology
  • Biochemistry
  • Organic Chemistry

Background:

  • Peptide and protein modification is crucial for biological research.
  • Enzymatic hydrolysis is a common method for macromolecule degradation.
  • Site-selective chemical cleavage offers complementary control over degradation.

Purpose of the Study:

  • To review recent advancements in site-selective chemical peptide bond cleavage.
  • To emphasize the mechanisms underlying these chemical methods.
  • To discuss the implications for reactivity, selectivity, and substrate scope.

Main Methods:

  • Literature review of chemical cleavage methods.
  • Analysis of postulated reaction mechanisms.
  • Evaluation of selectivity and substrate scope in reported studies.

Main Results:

  • Overview of various chemical strategies for site-selective peptide cleavage.
  • Discussion of mechanistic insights into reactivity and selectivity.
  • Assessment of the applicability of these methods across different peptide and protein substrates.

Conclusions:

  • Chemical site-selective cleavage is a powerful tool for macromolecule modification.
  • Understanding reaction mechanisms is key to optimizing selectivity and scope.
  • Continued development promises broader applications in chemical biology.