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Human acyl-CoA thioesterase 7

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PDB Code 2QQ2 Target Class Lipid signalling Target ACOT7 Alias ACH1, ACOT7, ACT, BACH, CTE-II, hBACH, LACH, LACH1, MGC1126, RP1-120G22.10 Disease Area/Function metabolism Date Deposited Jul 26 2007 Authors BUSAM, R., LEHTIO, L., ARROWSMITH, C., BERGLUND, H., COLLINS, R., DAHLGREN, L.G., HERMAN, M.D., EDWARDS, A., FLODIN, S., FLORES, A., GRASLUND, S., HAMMARSTROM, M., HALLBERG, B.M., HOLMBERG-SCHIAVONE, L., JOHANSSON, I., KALLAS, A., KARLBERG, T., KOTENYOVA, T., MOCHE, M., NORDLUND, P., NYMAN, T., SAGEMARK, J., STENMARK, P., SUNDSTROM, M., THORSELL, A.G., TRESAUGUES, L., VAN DEN BERG, S., WEIGELT, J., WELIN, M., PERSSON, C.

About this structure

Acyl-CoA thioesterases is a family of ezymes that hydrolyzes acyl-CoA to the free fatty acid and coenzyme A. Acyl-CoA thioesterase 7 (ACOT7 or BACH) catalyses acyl-CoA hydrolysis with broad chain-length specificity, hydrolysing acyl-CoAs with carbon numbers C6-C22 and has high specificity for arachidonoyl-CoA. ACOT7 expression is induced during embryogenesis in association with neuronal differentiation, and persists after terminal differentiation into neurons in postnatal stages. Decreased expression of this gene may be associated with drug-resistant mesial temporal lobe epilepsy. Gene transcription is activated by sterol regulatory element-binding protein 2 suggesting that ACOT7 has a function in cholesterol metabolism. The protein contains two thioesterase domains in tandem with 30% sequence identity. It has been shown that both domains are required for activity. We have determined the structure of the C-terminal domain of ACOT7, which displays a hot-dog fold typical for this enzyme family.

References

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