Literature summary for 3.1.2.2 extracted from

Cheng, F.; Wang, Q.; Chen, M.; Quiocho, F.A.; Ma, J.
Molecular docking study of the interactions between the thioesterase domain of human fatty acid synthase and its ligands (2008), Proteins, 70, 1228-1234.

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Inhibitors

Inhibitors	Comment	Organism	Structure
C75	binds the thioesterase domain in a similar orientation to that of palmitate, with its hydrophobic group buried inside the distal pocket and hydrophilic group interacting with the catalytic triad	Homo sapiens
orlistat	in the lowest-energy conformation, its central formylamino group is very close to the catalytic triad of the thioesterase domain. Its shorter chain is placed into the distal pocket where palmitate acyl chain binds and its longer chain extends into pocket 2	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the ligand binding pocket of the thioesterase domain is a decisive factor in chain length specificity	Homo sapiens	?	-	?
palmitoyl-CoA + H2O	ligand-binding pocket of the thioesterase domain encompasses the catalytic triad of Ser2308, His2481, Asp2338. The hydrophobic interactions are the major decisive factor for the optimal binding of the alphatic chain of palmitate	Homo sapiens	CoA + palmitate	-	?

Synonyms

Synonyms	Comment	Organism
FAS	-	Homo sapiens
fatty acid synthase thioesterase	-	Homo sapiens

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Release 2023.1 (January 2023)