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Related Concept Videos

Peptide Bonds02:43

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
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Protein Digestion01:02

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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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Related Experiment Video

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Identification of Kinase-substrate Pairs Using High Throughput Screening
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Demystifying O-GlcNAcylation: hints from peptide substrates.

Jie Shi1, Rob Ruijtenbeek1,2, Roland J Pieters1

  • 1Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, TB Utrecht, The Netherlands.

Glycobiology
|April 11, 2018
PubMed
Summary
This summary is machine-generated.

O-GlcNAcylation, a vital protein modification, is studied using peptide substrates. These peptides offer insights into O-GlcNAc transferase and O-GlcNAcase enzymes, aiding disease research and therapeutic development.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Post-Translational Modifications
  • Enzymology

Background:

  • O-GlcNAcylation is a dynamic protein modification analogous to phosphorylation, regulating cellular processes.
  • Deregulation of O-GlcNAcylation is linked to chronic diseases like cancer, diabetes, and neurodegenerative disorders.
  • O-GlcNAc transferase and O-GlcNAcase are the sole enzymes governing O-GlcNAc attachment and removal.

Purpose of the Study:

  • To review recent advancements in studying O-GlcNAcylation and deglycosylation at the peptide level.
  • To highlight the utility of peptide substrates in understanding O-GlcNAc processing enzymes.
  • To explore the therapeutic potential of O-GlcNAc processing enzymes and peptide substrate-inspired inhibitors.

Main Methods:

  • Utilizing peptide substrates derived from natural O-GlcNAcylation targets.
  • Applying peptide chemistry to study enzyme activity and regulatory mechanisms.
  • Investigating enzyme specificity and direct function through peptide-based approaches.

Main Results:

  • Peptide substrates serve as ideal models for studying O-GlcNAcylation and deglycosylation enzymes.
  • Recent progress has advanced the understanding of enzyme specificities and regulatory mechanisms.
  • Peptide studies have identified potential therapeutic targets and informed the design of inhibitors.

Conclusions:

  • Peptide-level studies are crucial for a deeper understanding of O-GlcNAc processing enzymes.
  • O-GlcNAc processing enzymes and their modulators represent promising therapeutic targets for related diseases.
  • Future research leveraging peptide chemistry will continue to advance the field of O-GlcNAcylation.