User:Cassandra Marsh/Sandbox 1

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===Histone Deacetylases (HDACs)===
===Histone Deacetylases (HDACs)===
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ε-Amino-lysine acetylation is a type of modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni" />. There are different classes of HDACs based on phylogenetic analysis:
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ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">doi: :10.1038/sj.embor.7401047</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3
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•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1 <ref name="Vanninni">doi: :10.1038/sj.embor.7401047</ref>.
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•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1
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•Class III - Sirtuin deacetylases
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•Class IV - HDAC 11 <ref name="Vanninni" />.
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />.
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />.

Revision as of 16:43, 6 April 2019

Histone Deacetylase 8 (HDAC 8), H. sapians

HDAC 8 (PDB:2v5w)

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References

  1. ↑ 1.0 1.1 1.2 Histones | Learn Science at Scitable https://www.nature.com/scitable/definition/histone-histones-57
  2. ↑ 2.0 2.1 2.2 . PMID:216315890657

Student Contributors

  • Cassandra Marsh
  • Courtney Brown
  • Carolyn Hurdle

Proteopedia Page Contributors and Editors (what is this?)

Cassandra Marsh

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