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Related Concept Videos

Covalently Linked Protein Regulators02:04

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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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Histone Modification

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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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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Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Enzymatic lysine oxidation as a posttranslational modification.

Gemma Serra-Bardenys1, Sandra Peiró1

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Lysyl oxidase (LOX) enzymes regulate protein carbonylation, a key oxidative modification. This review details how LOX-mediated post-translational modifications impact protein function and interactions.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Post-translational Modifications

Background:

  • Oxidoreductases are a large enzyme class catalyzing oxidation-reduction reactions.
  • Protein carbonylation, forming aldehyde/keto groups on lysine residues, is a significant oxidative modification.
  • Carbonylation affects protein structure, function, localization, and interactions.

Purpose of the Study:

  • To review copper-dependent amine oxidases, focusing on the lysyl oxidase (LOX) family.
  • To discuss LOX-regulated oxidation reactions involving lysine residues.
  • To summarize novel substrates and the regulatory roles of LOX-mediated post-translational modifications.

Main Methods:

  • Literature review of oxidoreductases and protein carbonylation.
  • Focus on copper-dependent amine oxidases and the lysyl oxidase (LOX) family.
  • Analysis of post-translational modification mechanisms and functional consequences.

Main Results:

  • Lysyl oxidase (LOX) enzymes catalyze oxidative deamination of amines to aldehydes.
  • LOX-mediated carbonylation of lysine residues is a critical post-translational modification.
  • This modification influences protein function, stability, localization, and interactions.

Conclusions:

  • Lysyl oxidase (LOX) family proteins play a crucial role in protein carbonylation.
  • Understanding LOX-mediated modifications provides insights into protein regulation.
  • Further research on LOX substrates and functions is warranted.