Ubiquitin

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Ubiquitin ligase is a [[Protein|protein]] which is found in all [[Eukaryotic|eukaryotic]] [[Cell|cells]]. Ubiqiutin allows cells to recognise the proteins that need to be degraded by binding on the protein. This binding of ubiquitin to the protein labels the proteins for destruction. The enzymes are involved in the binding of ubiquitin to a protein, [[Ubiquitin-activating enzyme|ubiquitin-activating enzyme]] ([[Ubiquitin-activating enzyme E1|E1]]), ubiquitin-conjugating enzyme ([[Ubiquitin-activating enzyme E2|E2]]) and ubiquitin-protein ligase ([[Ubiquitin-activating enzyme E3|E3]])<ref>Jeremy M. Berg,John L. Tymoczko, Lubert Stryer, 2011, Biochemistry,7 th edition,W.H. Freeman and Company.pg 699-700</ref>.  
 
Ubiquitin ligase is a [[Protein|protein]] which is found in all [[Eukaryotic|eukaryotic]] [[Cell|cells]]. Ubiqiutin allows cells to recognise the proteins that need to be degraded by binding on the protein. This binding of ubiquitin to the protein labels the proteins for destruction. The enzymes are involved in the binding of ubiquitin to a protein, [[Ubiquitin-activating enzyme|ubiquitin-activating enzyme]] ([[Ubiquitin-activating enzyme E1|E1]]), ubiquitin-conjugating enzyme ([[Ubiquitin-activating enzyme E2|E2]]) and ubiquitin-protein ligase ([[Ubiquitin-activating enzyme E3|E3]])<ref>Jeremy M. Berg,John L. Tymoczko, Lubert Stryer, 2011, Biochemistry,7 th edition,W.H. Freeman and Company.pg 699-700</ref>.  
  
Ubiquitin is a protein with a [[Globular protein|globular]] structure<ref>The University of Nottingham. The Pathway of Protein Ubiquitylation. [18/11/18]. Available from: https://www.Nottingham.ac.uk/biochemcourses/students/ub/ubpath.html</ref>., consisting of 76 [[Amino-acids|amino acid]] [[Amino acid residues|residues]]<ref>European Bioinformatics Institute. Jennifer McDowall. Ubiquitin. [15/11/18]. Available from: https://www.ebi.ac.uk/interpro/potm/2004_12/Page1.htm</ref>., linked by [[Peptide bond|peptide bonds]], that have been folded tightly into a compact structure. Ubiquitin is a part of the Ubiquitin system, which involves the process of [[Ubiquitination|ubiquitination]] which is the reversible<ref>NCBI. Viduth K. Chaugule and Helen Walden. Specificity and Disease in the Ubiquitin System. 2016. [18/11/18]. Available from: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5264512/</ref>&nbsp;alteration of the function of the location of a protein by the attachment of ubiquitin or leads to protein degradation.  
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Ubiquitin is a protein with a [[Globular protein|globular]] structure<ref>The University of Nottingham. The Pathway of Protein Ubiquitylation. [18/11/18]. Available from: https://www.Nottingham.ac.uk/biochemcourses/students/ub/ubpath.html</ref>, consisting of 76 [[Amino-acids|amino acid]] [[Amino acid residues|residues]]<ref>European Bioinformatics Institute. Jennifer McDowall. Ubiquitin. [15/11/18]. Available from: https://www.ebi.ac.uk/interpro/potm/2004_12/Page1.htm</ref>, linked by [[Peptide bond|peptide bonds]], that have been folded tightly into a compact structure. Ubiquitin is a part of the Ubiquitin system, which involves the process of [[Ubiquitination|ubiquitination]] which is the reversible<ref>NCBI. Viduth K. Chaugule and Helen Walden. Specificity and Disease in the Ubiquitin System. 2016. [18/11/18]. Available from: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5264512/</ref>&nbsp;alteration of the function of the location of a protein by the attachment of ubiquitin or leads to protein degradation.  
  
 
=== References  ===
 
=== References  ===
  
 
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Latest revision as of 18:35, 4 December 2018

Ubiquitin ligase is a protein which is found in all eukaryotic cells. Ubiqiutin allows cells to recognise the proteins that need to be degraded by binding on the protein. This binding of ubiquitin to the protein labels the proteins for destruction. The enzymes are involved in the binding of ubiquitin to a protein, ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2) and ubiquitin-protein ligase (E3)[1].

Ubiquitin is a protein with a globular structure[2], consisting of 76 amino acid residues[3], linked by peptide bonds, that have been folded tightly into a compact structure. Ubiquitin is a part of the Ubiquitin system, which involves the process of ubiquitination which is the reversible[4] alteration of the function of the location of a protein by the attachment of ubiquitin or leads to protein degradation.

References

  1. Jeremy M. Berg,John L. Tymoczko, Lubert Stryer, 2011, Biochemistry,7 th edition,W.H. Freeman and Company.pg 699-700
  2. The University of Nottingham. The Pathway of Protein Ubiquitylation. [18/11/18]. Available from: https://www.Nottingham.ac.uk/biochemcourses/students/ub/ubpath.html
  3. European Bioinformatics Institute. Jennifer McDowall. Ubiquitin. [15/11/18]. Available from: https://www.ebi.ac.uk/interpro/potm/2004_12/Page1.htm
  4. NCBI. Viduth K. Chaugule and Helen Walden. Specificity and Disease in the Ubiquitin System. 2016. [18/11/18]. Available from: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5264512/
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