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An acetyl group contains a methyl group (−CH 3) that is single-bonded to a carbonyl (C=O), making it an acyl group. The carbonyl center of an acyl radical has one non-bonded electron with which it forms a chemical bond to the remainder (denoted with the letter R ) of the molecule.
Acetyl-CoA (acetyl coenzyme A) is a molecule that participates in many biochemical reactions in protein, carbohydrate and lipid metabolism. [2] Its main function is to deliver the acetyl group to the citric acid cycle (Krebs cycle) to be oxidized for energy production.
HAT molecules facilitate the transfer of an acetyl group from a molecule of acetyl-coenzyme A (Acetyl-CoA) to the NH 3 + group on lysine. When a lysine is to be deacetylated, factors known as histone deacetylases (HDACs) catalyze the removal of the acetyl group with a molecule of H 2 O. [3] [4]
It introduces an acetyl group into a chemical compound. Such compounds are termed acetate esters or simply acetates. Deacetylation is the opposite reaction, the removal of an acetyl group from a chemical compound.
In its acetyl form, coenzyme A is a highly versatile molecule, serving metabolic functions in both the anabolic and catabolic pathways. Acetyl-CoA is utilised in the post-translational regulation and allosteric regulation of pyruvate dehydrogenase and carboxylase to maintain and support the partition of pyruvate synthesis and degradation. [3]
It also contains an ester functional group (in red), and an acetyl functional group (encircled with dark green). Other divisions can be made. In organic chemistry, a moiety (/ ˈ m ɔɪ ə t i / MOY-ə-tee) is a part of a molecule [1] [2] that is given a name because it is identified as a part of other molecules as well.
Acyl-CoA is a group of CoA-based coenzymes that metabolize carboxylic acids. Fatty acyl-CoA's are susceptible to beta oxidation, forming, ultimately, acetyl-CoA. The acetyl-CoA enters the citric acid cycle, eventually forming several equivalents of ATP. In this way, fats are converted to ATP, the common biochemical energy carrier.
Acetyl-CoA binds first, followed by the histone substrate. A conserved glutamate residue (Glu173 in yeast Gcn5) activates a water molecule for removal of a proton from the amine group on lysine, which activates it for direct nucleophilic attack on the carbonyl carbon of enzyme-bound acetyl-CoA.