Search results
Results From The WOW.Com Content Network
Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle.All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate.
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.
Coenzyme A transferases (CoA-transferases) are transferase enzymes that catalyze the transfer of a coenzyme A group from an acyl-CoA donor to a carboxylic acid acceptor. [ 1 ] [ 2 ] Among other roles, they are responsible for transfer of CoA groups during fermentation and metabolism of ketone bodies .
Three types of acyl-CoA synthases are employed, depending on the chain length of the fatty acid. [3] For example, the substrates for medium chain acyl-CoA synthase are 4-11 carbon fatty acids. [4] The enzyme acyl-CoA thioesterase takes of the acyl-CoA to form a free fatty acid and coenzyme A. [4]
The systematic name of this enzyme class is acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase. Other names in common use include acetyl coenzyme A-acyl-carrier-protein transacylase, acetyl-CoA:ACP transacylase, [acyl-carrier-protein]acetyltransferase, [ACP]acetyltransferase, and ACAT. This enzyme participates in fatty acid biosynthesis.
The systematic name of this enzyme class is acetyl-CoA:acetyl-CoA C-acetyltransferase. Other names in common use include acetoacetyl-CoA thiolase , beta-acetoacetyl coenzyme A thiolase , 2-methylacetoacetyl-CoA thiolase [misleading] , 3-oxothiolase , acetyl coenzyme A thiolase , acetyl-CoA acetyltransferase , acetyl-CoA:N-acetyltransferase ...
FAD is bound between the three domains of the monomer, where only the nucleotide portion is accessible. FAD binding contributes significantly to overall enzyme stability. The acyl-CoA substrate is bound completely within each monomer of the enzyme. The active site is lined with the residues F252, T255, V259, T96, T99, A100, L103, Y375, Y375 ...
In enzymology, an acetate CoA-transferase (EC 2.8.3.8) is an enzyme that catalyzes the chemical reaction. acyl-CoA + acetate a fatty acid anion + acetyl-CoA. Thus, the two substrates of this enzyme are acyl-CoA and acetate, whereas its two products are long-chain carboxylate anion and acetyl-CoA.