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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.
Carnitine O-acetyltransferase also called carnitine acetyltransferase (CRAT, or CAT) [5] (EC 2.3.1.7) is an enzyme that encoded by the CRAT gene that catalyzes the chemical reaction. acetyl-CoA + carnitine CoA + acetylcarnitine. where the acetyl group displaces the hydrogen atom in the central hydroxyl group of carnitine.
In yeast, acyl-CoA:sterol acyltransferase (ASAT) is functionally equivalent to ACAT. Although studies in vitro and in yeast suggest that the acyl-CoA binding protein (ACBP) may modulate long-chain fatty acyl-CoA (LCFA-CoA) distribution, the physiological function in mammals is unresolved. Recent research suggests that ACBP expression may play a ...
Cytosolic citrate, meaning citrate in the cytosol, is a key substrate for the generation of energy. It releases acetyl-CoA and provides NADPH for fatty acid synthesis, and, in subsequent pathways, generates NAD + for glycolysis. Citrate also activates acetyl-CoA carboxylase, an enzyme that is essential in the fatty acid synthesis pathway. [11]
3-Ketoacyl-CoA thiolase, mitochondrial also known as acetyl-Coenzyme A acyltransferase 2 is an enzyme that in humans is encoded by the ACAA2 gene. [ 5 ] [ 6 ] Acetyl-Coenzyme A acyltransferase 2 is an acetyl-CoA C-acyltransferase enzyme.
The biotin carboxyl carrier protein is an Acetyl CoA subunit that allows for Acetyl CoA to be catalyzed and converted to malonyl-CoA. More specifically, BCCP catalyzes the carboxylation of the carrier protein to form an intermediate. Then the carboxyl group is transferred by the transcacrboxylase to form the malonyl-CoA. [1]
In enzymology, a serine O-acetyltransferase (EC 2.3.1.30) is an enzyme that catalyzes the chemical reaction. acetyl-CoA + L-serine CoA + O-acetyl-L-serine Thus, the two substrates of this enzyme are acetyl-CoA and L-serine, whereas its two products are CoA and O-acetyl-L-serine.
The mechanism of the enzyme requires removal of the α-proton of the 2-methylacyl-CoA to form a deprotonated intermediate (which is probably the enol or enolate [10]) followed by non-sterespecific reprotonation. [11] Thus either epimer is converted into a near 1:1 mixture of both isomers upon full conversion of the substrate.