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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
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Role of extracellular GAPDH in Streptococcus pyogenes virulence.

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Basic biology of GAPDH.

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GAPDH and intermediary metabolism.

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Related Experiment Video

Updated: May 20, 2026

Chemoselective Modification of Viral Surfaces via Bioorthogonal Click Chemistry
12:31

Chemoselective Modification of Viral Surfaces via Bioorthogonal Click Chemistry

Published on: August 19, 2012

Target for diverse chemical modifications.

Norbert W Seidler1

  • 1Department of Biochemistry, Kansas City University of Medicine and Biosciences, Kansas City, MO, USA.

Advances in Experimental Medicine and Biology
|August 2, 2012
PubMed
Summary
This summary is machine-generated.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) exists as a single functional gene but exhibits multiple forms due to post-translational modifications and non-enzymatic reactions. Misfolded GAPDH may compromise cellular function by blocking chaperonins.

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Last Updated: May 20, 2026

Chemoselective Modification of Viral Surfaces via Bioorthogonal Click Chemistry
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Published on: April 26, 2024

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key glycolytic enzyme.
  • Despite a single functional somatic gene in humans, multiple GAPDH forms have been reported.
  • GAPDH is susceptible to various post-translational modifications and non-enzymatic reactions.

Purpose of the Study:

  • To provide a historical perspective on GAPDH isozymes.
  • To discuss the factors contributing to GAPDH heterogeneity.
  • To explore the role of GAPDH in cellular stress and decline.

Main Methods:

  • Literature review of GAPDH research.
  • Analysis of post-translational modifications.
  • Discussion of non-enzymatic reactions affecting GAPDH.
  • Exploration of GAPDH interactions with chaperonins.

Main Results:

  • GAPDH heterogeneity arises from enzymatic modifications and non-enzymatic reactions like oxidation and nitration.
  • Metabolic gases (nitric oxide, hydrogen sulfide) signal via non-enzymatic reactions with GAPDH.
  • Misfolded GAPDH may impair cellular function by inhibiting chaperonins.

Conclusions:

  • GAPDH's susceptibility to modifications and reactions contributes to its functional diversity.
  • GAPDH plays a role in cellular stress responses and signaling pathways.
  • Dysfunctional GAPDH, potentially through chaperonin interaction, is implicated in cellular decline.