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In organic chemistry, thioesters are organosulfur compounds with the molecular structure R−C(=O)−S−R’. They are analogous to carboxylate esters ( R−C(=O)−O−R’ ) with the sulfur in the thioester replacing oxygen in the carboxylate ester, as implied by the thio- prefix.
Thioester containing protein 1, often called TEP1 is a key component of the arthropod innate immune system. TEP1 was first identified as a key immunity gene in 2001 through functional studies on Anopheles gambiae mosquitoes.
To participate in specific metabolic processes, fatty acids must first be activated by being joined in thioester linkage (R-CO-SCoA) to the -SH group of coenzyme A, where R is a fatty carbon chain. The thioester bond is a high energy bond. [1] The activation reaction normally occurs in the endoplasmic reticulum or the outer mitochondrial membrane.
A conserved, classical catalytic triad to break ester and thioester bonds; [2] 2. A long hydrophobic substrate tunnel to accommodate the palmitoyl moiety, as identified in the crystal structures of human acyl-protein thioesterase 1, [2] human acyl-protein thioesterase 2 [13] and Zea mays acyl-protein thioesterase 2; [14] 3.
Pages in category "Thioesters" The following 24 pages are in this category, out of 24 total. This list may not reflect recent changes. ...
Palmitoyl protein hydrolase/thioesterases is an enzyme (EC 3.1.2.22) that removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. It catalyzes the reaction palmitoyl[protein] + H 2 O palmitate + protein
Succinyl-coenzyme A, abbreviated as succinyl-CoA (/ ˌ s ʌ k s ɪ n əl ˌ k oʊ ˈ eɪ /) or SucCoA, is a thioester of succinic acid and coenzyme A. Sources
This thioester linkage is a "high energy" bond, which is particularly reactive. Hydrolysis of the thioester bond is exergonic (−31.5 kJ/mol). CoA is acetylated to acetyl-CoA by the breakdown of carbohydrates through glycolysis and by the breakdown of fatty acids through β-oxidation.