Acetyltransferase

Acetyltransferase (or transacetylase) is a type of transferase enzyme that transfers an acetyl group. Examples include:

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

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 proteinprotein interaction domains, such as the acetyl-lysine-binding bromodomain.Histone acetyltransferases can also acetylate non-histone proteins, such as transcription factors and nuclear receptors to facilitate gene expression.

CREB-binding protein
CREB-binding protein, also known as CREBBP or CBP, is a protein that in humans is encoded by the CREBBP gene. The CREB protein carries out its function by activating transcription, where interaction with transcription factors is managed by one or more of p300 domains: the nuclear receptor interaction domain (RID), the CREB and MYB interaction domain (KIX), the cysteine/histidine regions (TAZ1/CH1 and TAZ2/CH3) and the interferon response binding domain (IBiD). The CREB protein domains, KIX, TAZ1 and TAZ2, each bind tightly to a sequence spanning both transactivation domains 9aaTADs of transcription factor p53.

Function
This gene is ubiquitously expressed and is involved in the transcriptional coactivation of many different transcription factors. First isolated as a nuclear protein that binds to cAMP-response element-binding protein (CREB), this gene is now known to play critical roles in embryonic development, growth control, and homeostasis by coupling chromatin remodeling to transcription factor recognition. The protein encoded by this gene has intrinsic histone acetyltransferase activity and also acts as a scaffold to stabilize additional protein interactions with the transcription complex. This protein acetylates both histone and non-histone proteins. This protein shares regions of very high-sequence similarity with protein EP300 in its bromodomain, cysteine-histidine-rich regions, and histone acetyltransferase domain. Recent results suggest that novel CBP-mediated post-translational N-glycosylation activity alters the

conformation of CBP-interacting proteins, leading to regulation of gene expression, cell growth and differentiation

Choline acetyltransferase
Choline acetyltransferase (abbreviated "ChAT") is an enzyme that is synthesized within the body of a neuron. It is then transferred to the nerve terminal via axoplasmic flow. The role of choline acetyltransferase is to join Acetyl-CoA to choline, resulting in the formation of the neurotransmitter acetylcholine.[In humans, the choline acetyltransferase enyzme is encoded by the CHAT gene.

Function
Cholinergic systems are implicated in numerous neurologic functions. Alteration in some cholinergic neurons may account for the disturbances of Alzheimer disease. The protein encoded by this gene synthesizes the neurotransmitter acetylcholine. Alternative splice variants that contain alternative 5' untranslated exons have been found. Three of the four described splice variants encode identical 69 kDa proteins, while one variant encodes both the 69 kDa and a larger 82 kDa protein.

Chloramphenicol acetyltransferase
Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. The crystal structure of the type III enzyme from Escherichia coli with chloramphenicol bound has been determined. CAT is a trimer of identical subunits (monomer Mr 25,000) and the trimeric structure is stabilised by a number of hydrogen bonds, some of which result in the extension of a beta-sheet across the subunit interface. Chloramphenicol binds in a deep pocket located at the boundary between adjacent subunits of the trimer, such that the majority of residues forming the binding pocket belong to one subunit while the catalytically essential histidine belongs to the adjacent subunit. His195 is appropriately positioned to act as a general base catalyst in the reaction, and the required tautomeric stabilisation is provided by an unusual interaction with a main-chain carbonyl oxygen.

Application
CAT is used as a reporter system to measure the level of a promoter or its tissuespecific expression. The CAT assay involves monitoring acetylation of radioactive chloramphenicol on a TCA plate; we determine CAT activity by looking for one or both of the two acetylated forms of chloramphenicol, which have a significantly increased migration rate as compared to the unacetylated form.

Serotonin N-acetyl transferase

Serotonin N-acetyl transferase also known as arylalkylamine N-acetyltransferase or AANAT is a protein that, in humans, is encoded by the AANAT gene.

Function
The protein encoded by this gene is an enzyme involved in the conversion of serotonin to melatonin in pinealocytes. It is an acetyl-CoA-dependent enzyme of the GCN5-related family of N-acetyltransferases (GNATs). Arylalkylamine N-acetyltransferase is the penultimate enzyme in melatonin synthesis and controls the night/day rhythm in melatonin production in the vertebrate pineal gland. Melatonin is essential for seasonal reproduction, modulates the function of the circadian clock in the suprachiasmatic nucleus, and influences activity and sleep. This enzyme is rapidly inactivated when animals are exposed to light at night. This protein is 80% identical to sheep and rat AANAT. Arylalkylamine N-acetyltransferase may contribute a multifactorial genetic diseases such as altered behavior in sleep/wake cycle.

Students name: Phm Anh Ho ID: BTIU09055