Synonyms for acetylate or Related words with acetylate

deacetylate              esterify              acetylates              dephosphorylate              esterifies              deacylate              hydrolyse              deprotect              propionylated              deacetylating              hydroxylate              deacetylated              succinylation              hydrolizes              etherify              propionylation              biotinylate              demethylate              ethoxycarbonylation              ribosylated              hydrolize              formylated              unacetylated              glucosylate              prenylcysteine              adenylating              solubilise              epoxysuccinyl              acetylating              transaminated              maleylation              deprotonate              xxkxxxk              derivatize              deaminated              succinylated              anddeprotecting              deacetylates              esterificated              expoxide              sulphydryl              hydrolized              dihydronootkatone              trifluoroacetylated              butyrylated              iodinate              autophosphorylate              protonate              chemoselectively              depolymerize             

Examples of "acetylate"
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.
Different HATs, usually in the context of multisubunit complexes, have been shown to acetylate specific lysine residues in histones.
p300/CBP acetylate all four nucleosomal core histones equally well. "In vitro", they have been observed to acetylate H2AK5, H2BK12, H2BK15, H3K14, H3K18, H4K5, and H4K8. SRC-1 acetylates H3K9 and H3K14, TAF230 (Drosophila homolog of human TAF250) acetylates H3K14, and Rtt109 acetylates H3K9, H3K23, and H3K56 in the presence of either Asf1 or Vps75.
PCAF forms complexes with numerous proteins that guide its activity. For example PCAF is recruited by ATF to acetylate histones and promote transcription of ATF4 target genes.
Gcn5 cannot acetylate nucleosomal histones in the absence of other protein factors. In the context of complexes like SAGA and ADA, however, Gcn5 is able to acetylate H3K14 among other sites within histones H2B, H3, and H4 (e.g., H3K9, H3K36, H4K8, H4K16). Both Gcn5 and PCAF have the strongest site preference for H3K14, either as a free histone or within a nucleosome. Hat1 acetylates H4K5 and H4K12, and Hpa2 acetylates H3K14 "in vitro".
In flies, acetylation of H4K16 on the male X chromosome by MOF in the context of the MSL complex is correlated with transcriptional upregulation as a mechanism for dosage compensation in these organisms. In humans, the MSL complex carries out the majority of genome-wide H4K16 acetylation. In the context of their cognate complexes, Sas2 (SAS) and Esa1 (NuA4) also carry out acetylation of H4K16, in particular in the telomere regions of chromosomes. Sas2 is also observed to acetylate H3K14 "in vitro" on free histones. Esa1 can also acetylate H3K14 "in vitro" on free histones as well as H2AK5, H4K5, H4K8, and H4K12 either "in vitro" or "in vivo" on nucleosomal histones. H2AK7 and H2BK16 are also observed to be acetylated by Esa1 "in vivo". Notably, neither Sas2 nor Esa1 can acetylate nucleosomal histones "in vitro" as a free enzyme. This happens to be the case as well for Sas3, which is observed to acetylate H3K9 and H3K14 "in vivo" as well as lysine residues on H2A and H4. MOZ can also acetylate H3K14.
General Control Non-Derepressible 5 (Gcn5) –related N-Acetyltransferases (GNATs) is one of the many studied families with acetylation abilities. This superfamily includes the factors Gcn5 which is included in the SAGA, SLIK, STAGA, ADA, and A2 complexes, Gcn5L, p300/CREB-binding protein associated factor (PCAF), Elp3, HPA2 and HAT1. Major features of the GNAT family include HAT domains approximately 160 residues in length and a conserved bromodomain that has been found to be an acetyl-lysine targeting motif. Gcn5 has been shown to acetylate substrates when it is part of a complex. Recombinant Gcn5 has been found to be involved in the acetylation of the H3 histones of the nucleosome. To a lesser extent, it has been found to also acetylate H2B and H4 histones when involved with other complexes. PCAF has the ability to act as a HAT protein and acetylate histones, it can acetylate non-histone proteins related to transcription, as well as act as a coactivator in many processes including myogenesis, nuclear-receptor-mediated activation and growth-factor-signaled activation. Elp3 has the ability to acetylate all histone subunits and also shows involvement in the RNA polymerase II holoenzyme.
The production of black tar heroin results in significant amounts of 6-MAM in the final product. 6-MAM is approximately 30 percent more active than diacetylmorphine itself, This is why despite lower heroin content, black tar heroin may be more potent than some other forms of heroin. 6-MAM can be synthesized from morphine using glacial acetic acid with an organic base as a catalyst. The acetic acid must be of a high purity (97-99 per cent) for the acid to properly acetylate the morphine at the 6th position effectively creating 6-MAM. Acetic acid is used rather than acetic anhydride, as acetic acid is not strong enough to acetylate the phenolic 3-hydroxy group but is able to acetylate the 6-hydroxy group, thus selectively producing 6-MAM rather than heroin. Acetic acid is a convenient way to produce 6-MAM, as acetic acid also is not a watched chemical as it is the main component of vinegar.
HATs are enzymes responsible for the acetylation of amino acids. 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. HAT enzymes are most often associated with histone proteins and work to regulate the interaction between histones and the DNA that is wrapped around them. 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.
The formation of multisubunit complexes has been observed to modulate the substrate specificity of HATs. In general, while recombinant HATs are able to acetylate free histones, HATs can acetylate nucleosomal histones only when they are in their respective "in vivo" HAT complexes. Some of the proteins that associate with HATs in these complexes function by targeting the HAT complex to nucleosomes at specific regions in the genome. For instance, it has been observed that HAT complexes (e.g. SAGA, NuA3) often use methylated histones as docking sites so that the catalytic HAT subunit can carry out histone acetylation more effectively.
Adenoviral E1A-associated protein of 300kDa (p300) and the CREB-binding protein (CBP) make up the next family of HATs. This family of HATs contain HAT domains that are approximately 500 residues long and contain bromodomains as well as three cysteine-histidine rich domains that help with protein interactions. These HATs are known to acetylate all of the histone subunits in the nucleosome. They also have the ability to acetylate and mediate non-histone proteins involved in transcription and are also involved in the cell-cycle, differentiation and apoptosis.
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. DNA is wrapped around histones, and, by transferring an acetyl group to the histones, genes can be turned on and off. In general, histone acetylation increases gene expression.
Sirtuin 1 is downregulated in cells that have high insulin resistance and inducing its expression increases insulin sensitivity, suggesting the molecule is associated with improving insulin sensitivity. Furthermore, SIRT1 was shown to de-acetylate and affect the activity of both members of the PGC1-alpha/ERR-alpha complex, which are essential metabolic regulatory transcription factors.
PCAF and p300/CBP are the main HATs that have been observed to acetylate a number of non-histone proteins. For PCAF, these include the non-histone chromatin (high-mobility group (HMG)) proteins HMG-N2/HMG17 and HMG-I(Y), the transcriptional activators p53, MyoD, E2F(1-3), and HIV Tat, and the general transcription factors TFIIE and TFIIF. Other proteins include CIITA, Brm (chromatin remodeler), NF-κB (p65), TAL1/SCL, Beta2/NeuroD, C/EBPβ, IRF2, IRF7, YY1, KLF13, EVI1, AME, ER81, and the androgen receptor (AR). PCAF has also been observed to acetylate c-MYC, GATA-2, retinoblastoma (Rb), Ku70, and E1A adenovirus protein. It can also autoacetylate, which facilitates intramolecular interactions with its bromodomain that may be involved in the regulation of its HAT activity.
Cumulative evidence suggests that such code is written by specific enzymes which can (for example) methylate or acetylate DNA ('writers'), removed by other enzymes having demethylase or deacetylase activity ('erasers'), and finally readily identified by proteins (‘readers’) that are recruited to such histone modifications and bind via specific domains, e.g., bromodomain, chromodomain. These triple action of ‘writing’, ‘reading’ and ‘erasing’ establish the favorable local environment for transcriptional regulation, DNA-damage repair, etc.
There are multiple studies that link FAM83A overexpression to lung, prostate, and bladder cancers. Researchers believe that this gene might make a good candidate for early detection of these cancers, especially lung cancer. It is unknown why or how FAM83A is upregulated. Studies have shown that arsenic can acetylate the promoter causing upregulation, suggesting this may be a similar mechanism to how this gene becomes unregulated in cancer.
Histone Acetyltransferases, also known as HATs, are a family of enzymes that acetylate the histone tails of the nucleosome. This, and other modifications, are expressed based on the varying states of the cellular environment. Many proteins with acetylating abilities have been documented and, after a time, were categorized based on sequence similarities between them. These similarities are high among members of a family, but members from different families show very little resemblance. Some of the major families identified so far are as follows.
In general, histone acetylation is linked to transcriptional activation and associated with euchromatin. When it was first discovered, it was thought that acetylation of lysine neutralizes the positive charge normally present, thus reducing affinity between histone and (negatively charged) DNA, which renders DNA more accessible to transcription factors. Research has emerged, since, to show that lysine acetylation and other posttranslational modifications of histones generate binding sites for specific protein–protein interaction domains, such as the acetyllysine-binding bromodomain. Histone acetyltransferases can also acetylate non-histone proteins, such as nuclear receptors and other transcription factors to facilitate gene expression.
The protein encoded by this gene is a type B histone acetyltransferase (HAT) that is involved in the rapid acetylation of newly synthesized cytoplasmic histones, which are, in turn, imported into the nucleus for de novo deposition onto nascent DNA chains. Histone acetylation, in particular, of histone H4, plays an important role in replication-dependent chromatin assembly. To be specific, this HAT can acetylate soluble but not nucleosomal histone H4 at lysines 5 and 12, and, to a lesser degree, histone H2A at lysine 5.
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. Acetylation of these proteins can alter their ability to interact with their cognate DNA and/or protein substrates. The idea that acetylation can affect protein function in this manner has led to inquiry regarding the role of acetyltransferases in signal transduction pathways and whether an appropriate analogy to kinases and phosphorylation events can be made in this respect.