Acetyltransferases are enzymes that catalyze the addition of acetyl moieties onto protein substrates. Histone acetyl transferases (HATs; a.k.a. histone acetylases) are a family of acetyltransferases that conjugate acetyl groups onto lysine residues of histones. Other types of acetyltransferases include: choline acetyltransferase (ChAT), NatA acetyltransferase, arylalkylamine N-acetyltransferase (AANAT) and arylamine N-acetyltransferase (NAT). ChAT is required for catalyzing the synthesis of acetylcholine, a neurotransmitter which functions in the CNS and PNS. NatA acetyltransferase acetylates proteins as they emerge from the ribosome. AANAT is involved in melatonin production and its activity is related to the circadian rhythm. NATs are a part of the phase II detoxification system and directly modify xenobiotic compounds such as drugs and carcinogens.
HATs associate with sequence specific transcription factors to target specific DNA regions, thus playing crucial roles in chromatin remodeling. They transfer acetyl groups onto the epsilon-amino position of lysine residues in histone tails resulting in localized chromatin relaxation. Therefore, acetylated chromatin regions are typically associated with gene activation. Aside from transcriptional activation, HATs are also involved in the DNA damage response by acetylating histones in damaged regions to facilitate the access of DNA repair enzymes; gene silencing and regulation of the cell cycle. Several HATs can also acetylate non-histone protein substrates such as transcription factors and these are generally referred to as lysine acetyltransferases (LATs).
Because they modify gene expression and DNA damage repair, HATs are key players in a wide range of biological pathways including those that control metabolic homeostasis, cell proliferation and differentiation, inflammation, circadian rhythm and cognitive function. As a result, HATs are implicated in many types of diseases such as breast cancer and gastrointestinal carcinogenesis. Moreover, recent studies have reported that reduced expression of the HAT CREB-binding protein (CBP) is associated with memory deficits in patients with Huntington's disease (HD). Taken together, HATs are promising therapeutic targets for pharmacological modulation to treat conditions such as metabolic syndrome, neurological disorders and cancer.
SignalChem offers a diverse and comprehensive range of active acetyltransferases and these can be used to perform acetylation reactions using a variety of substrate proteins, peptides and compounds.