acetylate

Gcn5 cannot acetylate nucleosomal histones in the absence of other protein factors.

Sas2 is also observed to acetylate H3K14 in vitro on free histones.

The enzymes usually phosphorylate, acetylate, or adenylate the drug compounds.

Ard1p - 27kDA, has catalytic properties which acetylate the nascent polypetide.

Recent studies have reported aspirin is able to acetylate several other targets in addition to COX isoenzymes.

In addition, the enzyme can be classified as an epigenic factor, because it has been found to acetylate histones as well.

Notably, neither Sas2 nor Esa1 can acetylate nucleosomal histones in vitro as a free enzyme.

Histone acetyltransferases can also acetylate non-histone proteins, such as transcription factors and nuclear receptors to facilitate gene expression.

Different HATs, usually in the context of multisubunit complexes, have been shown to acetylate specific lysine residues in histones.

Control experiments were performed to assess the ability of the Krebs-Henseleit saline, and also the supernatant of a cell suspension, to acetylate 5-ASA.

These complexes modulate HAT specificity by bringing HATs to their target genes where they can then acetylate nucleosomal histones.

PCAF and p300/CBP are the main HATs that have been observed to acetylate a number of non-histone proteins.

For example PCAF is recruited by ATF to acetylate histones and promote transcription of ATF4 target genes.

These HATs are generally characterized by the presence of a bromodomain, and they are found to acetylate lysine residues on histones H2B, H3, and H4.

HATs acetylate by converting the lysine side group of amino acids with the addition of an acetyl group from an acetyl CoA molecule, creating acetyl lysine.

HATs are not only restricted to the acetylation of histone but can also acetylate many other proteins implicated in the manipulation of gene expression like that of transcription factors and receptor proteins.

Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring an acetyl group from acetyl CoA to form ε-N-acetyllysine.

In addition to the core histones, certain HATs acetylate a number of other cellular proteins including transcriptional activators, basal transcription factors, structural proteins, polyamines, and proteins involved in nuclear import.

In contrast, Gcn5 acquires the ability to acetylate multiple sites in both histones H2B and H3 when it joins other subunits to form the SAGA and ADA complexes.

With N-acetyltransferases (involved in Phase II reactions), individual variation creates a group of people who acetylate slowly (slow acetylators) and those who acetylate quickly, split roughly 50:50 in the population of Canada.

Phosphorylation also allows for binding of transcriptional coactivators, like p300 or PCAF, which then acetylate the carboxy-terminal end of p53, exposing the DNA binding domain of p53, allowing it to activate or repress specific genes.

These HAT proteins are able to acetylate the amine group in the sidechain of histone lysine residues which makes lysine much less basic, not protonated at physiological pH, and therefore neutralizes the positive charges in the histone proteins.

In general, while recombinant HATs are able to acetylate free histones, HATs can only acetylate nucleosomal histones when they are in their respective in vivo HAT complexes.

Hoffmann, working at the Aktiengesellschaft Farbenfabriken (today the Bayer pharmaceutical company) in Elberfeld, Germany, was instructed by his supervisor Heinrich Dreser to acetylate morphine with the objective of producing codeine, a constituent of the opium poppy, pharmacologically similar to morphine but less potent and less addictive.