User:Megan Fleshman/Sandbox1
From Proteopedia
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==Introduction== | ==Introduction== | ||
ACAT is a [[http://en.wikipedia.org/wiki/Tetramer tetramer]] composed of a dimer of dimers. | ACAT is a [[http://en.wikipedia.org/wiki/Tetramer tetramer]] composed of a dimer of dimers. | ||
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+ | ==Mechanism== | ||
+ | The mechanism of the acyltransferase reaction occurs in the catalytic site one of the monomers in the dimer of ACAT1. The T tunnel and and C tunnel converge to the same space to allow the proper orientation of the Acyl CoA and the incoming cholesterol from the transmembrane. The Acyl CoA is oriented in a way to allow the His460 to act as a base catalyst to begin the reaction by deprotonation of the cholesterol which allows it to attack the carbonyl carbon which breaks the sulfur carbonyl bond (figure X). This mechanism produced Acyl-CoASH and cholesteryl ester. The Acyl-CcASH leaves through the C tunnel to the cytosol. | ||
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Crystal Structure of the Entamoeba histolytica RNA lariat debranching enzyme. <ref name=”Ransey”>PMID:28504306</ref> | Crystal Structure of the Entamoeba histolytica RNA lariat debranching enzyme. <ref name=”Ransey”>PMID:28504306</ref> |
Revision as of 20:58, 5 April 2021
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References
- ↑ Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:http://dx.doi.org/10.1002/1873-3468.12677
- ↑ Qian H, Zhao X, Yan R, Yao X, Gao S, Sun X, Du X, Yang H, Wong CCL, Yan N. Structural basis for catalysis and substrate specificity of human ACAT1. Nature. 2020 May;581(7808):333-338. doi: 10.1038/s41586-020-2290-0. Epub 2020 May, 13. PMID:32433614 doi:http://dx.doi.org/10.1038/s41586-020-2290-0
- ↑ Guan C, Niu Y, Chen SC, Kang Y, Wu JX, Nishi K, Chang CCY, Chang TY, Luo T, Chen L. Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor. Nat Commun. 2020 May 18;11(1):2478. doi: 10.1038/s41467-020-16288-4. PMID:32424158 doi:http://dx.doi.org/10.1038/s41467-020-16288-4
Student Contributors
- Megan Fleshman