Pathways & interactions
Acyl-CoA thioesterase, long chain (IPR016662)
Short name: Acyl-CoA_thioEstase_long-chain
Overlapping homologous superfamilies
- Alpha/Beta hydrolase fold (IPR029058)
Acyl-CoA thioesterases are a group of enzymes that catalyse the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH). They consequently have the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. They may also be involved in the metabolic regulation of peroxisome proliferation.
Thioesters play a central role in cells as they participate in metabolism, membrane synthesis, signal transduction, and gene regulation. Thioesterases catalyse the hydrolysis of thioesters to the thiol and carboxylic acid components. Many thioesterases have a hot dog fold, including YciA from Escherichia coli and its close sequence homologue HI0827 from Haemophilus influenzae (HiYciA) [PMID: 18247525].
In Helicobacter pylori, YbgC also belongs to the hot-dog family of proteins, with a epsilongamma tetrameric arrangement [PMID: 18338382]. YbgC proteins are bacterial acyl-CoA thioesterases associated with the Tol-Pal system. This system is important for cell envelope integrity and is part of the cell division machinery.
However, the E. coli thioesterase II reveals a new tertiary fold: a 'double hot dog'. It has an internal repeat with a basic unit that is structurally similar to the recently described beta-hydroxydecanoyl thiol ester dehydrase [PMID: 10876240].
This group represents a group of acyl-CoA thioesterases that predominantly hydrolyse long-chain acyl-CoA molecules.
- PIRSF016521 (Acyl-CoA_hydro)