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Covalently Linked Protein Regulators

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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.
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Overview of Fatty Acid Metabolism01:28

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Lipids also are sources of energy that power cellular processes. Like carbohydrates, lipids are composed of carbon, hydrogen, and oxygen, but these atoms are arranged differently. Most lipids are nonpolar and hydrophobic. Major types include fats and oils, waxes, phospholipids, and steroids.
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Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
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Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
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Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
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Ketohexokinase-C regulates global protein acetylation to decrease carnitine palmitoyltransferase 1a-mediated fatty

Robert N Helsley1, Se-Hyung Park2, Hemendra J Vekaria3

  • 1Department of Pediatrics and Gastroenterology, University of Kentucky, Lexington, KY, USA; Department of Pharmacology and Nutritional Sciences, University of Kentucky, Lexington, KY, USA; Saha Cardiovascular Research Center, University of Kentucky, Lexington, KY, USA; Markey Cancer Center, University of Kentucky, Lexington, KY, USA.

Journal of Hepatology
|February 23, 2023
PubMed
Summary
This summary is machine-generated.

Dietary fructose increases ketohexokinase-C (KHK-C), leading to protein acetylation that impairs fatty acid oxidation and promotes metabolic dysfunction. This reveals a novel mechanism linking sugar intake to obesity and related health issues.

Keywords:
FructoseKetohexokinaseNonalcoholic fatty liver diseaseSIRT2carnitine palmitoyltransferase 1afatty acid oxidationmass spectrometry

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Area of Science:

  • Metabolic research
  • Nutritional science
  • Molecular biology

Background:

  • High-fat diets (HFD) and sugar consumption contribute to obesity and metabolic dysfunction.
  • The synergistic mechanisms by which sugar exacerbates HFD-induced metabolic complications remain unclear.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which dietary fructose worsens metabolic dysfunction, particularly in the context of a HFD.
  • To investigate the role of ketohexokinase-C (KHK-C) and protein acetylation in mediating these effects.

Main Methods:

  • Mice were fed chow or HFD with varying sugar supplements (fructose, glucose).
  • Hepatocytes were engineered to overexpress KHK-C, and liver-specific CPT1α knockout mice were used.
  • Techniques included metabolomics, electron microscopy, proteomics, and acetylome analysis.

Main Results:

  • Fructose supplementation increased KHK-C, leading to elevated lipogenic proteins and CPT1α (carnitine palmitoyltransferase 1α) acetylation at K508.
  • KHK-C overexpression reduced CPT1α levels and increased triglyceride accumulation in vitro.
  • Increased KHK-C correlated with global protein acetylation and decreased SIRT2 (sirtuin 2) levels.

Conclusions:

  • KHK-C-induced protein acetylation is a novel mechanism by which dietary fructose promotes lipogenesis and reduces fatty acid oxidation.
  • These findings expand the understanding of sugar's metabolic impact beyond de novo lipogenesis and suggest therapeutic targets.