4zv3

Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7

Structural highlights

4zv3 is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Palmitoyl-CoA hydrolase, with EC number 3.1.2.2
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[BACH_MOUSE] Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA.^[1]

References

↑ Kuramochi Y, Takagi-Sakuma M, Kitahara M, Emori R, Asaba Y, Sakaguchi R, Watanabe T, Kuroda J, Hiratsuka K, Nagae Y, Suga T, Yamada J. Characterization of mouse homolog of brain acyl-CoA hydrolase: molecular cloning and neuronal localization. Brain Res Mol Brain Res. 2002 Jan 31;98(1-2):81-92. PMID:11834298

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OCA

[1] Kuramochi Y, Takagi-Sakuma M, Kitahara M, Emori R, Asaba Y, Sakaguchi R, Watanabe T, Kuroda J, Hiratsuka K, Nagae Y, Suga T, Yamada J. Characterization of mouse homolog of brain acyl-CoA hydrolase: molecular cloning and neuronal localization. Brain Res Mol Brain Res. 2002 Jan 31;98(1-2):81-92. PMID:11834298

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