Jump to content

Protein deacetylase

From Wikipedia, the free encyclopedia

This is the current revision of this page, as edited by Citation bot (talk | contribs) at 18:40, 11 July 2023 (Add: s2cid, pmid, authors 1-1. Removed parameters. Some additions/deletions were parameter name changes. | Use this bot. Report bugs. | #UCB_CommandLine). The present address (URL) is a permanent link to this version.

(diff) ← Previous revision | Latest revision (diff) | Newer revision → (diff)

A protein deacetylase is any enzyme that removes acetyl groups from lysine amino acids in proteins.[1]

The main ones are histone deacetylases (HDACs) and sirtuins (SIRT1,2,3,5).[2]

Because histone proteins were the first known substrate for protein deacetylases, the latter all tend to be called HDACs of one class or another.

Human protein deacetylase enzymes have been categorized into

  • Class I (HDAC1,2,3,8);
  • Class II (HDAC4,5,6,7,9,10),
  • Class III (SIRT1,2,3,5,6),
  • Class IV (HDAC11 and its related enzymes).

Class III are the NAD+-dependent protein deacetylases.

References

[edit]
  1. ^ "Protein Deacetylase - an overview | ScienceDirect Topics". www.sciencedirect.com. Retrieved 2023-03-16.
  2. ^ Gupta, Rohan; Ambasta, Rashmi K.; Kumar, Pravir (2022-01-01). "Multifaced role of protein deacetylase sirtuins in neurodegenerative disease". Neuroscience & Biobehavioral Reviews. 132: 976–997. doi:10.1016/j.neubiorev.2021.10.047. ISSN 0149-7634. PMID 34742724. S2CID 241905442.