Enzymes
| UniProtKB help_outline | 1,083 proteins |
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- Name help_outline (7Z)-octadecenoyl-CoA Identifier CHEBI:152050 Charge -4 Formula C39H64N7O17P3S InChIKeyhelp_outline IVOWZZDWEHGSGB-JUGOISETSA-J SMILEShelp_outline [C@@H]1(N2C3=C(C(=NC=N3)N)N=C2)O[C@H](COP(OP(OCC(C)([C@H](C(NCCC(NCCSC(=O)CCCCC/C=C\CCCCCCCCCC)=O)=O)O)C)(=O)[O-])(=O)[O-])[C@H]([C@H]1O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline cholesterol Identifier CHEBI:16113 (Beilstein: 2060565; CAS: 57-88-5) help_outline Charge 0 Formula C27H46O InChIKeyhelp_outline HVYWMOMLDIMFJA-DPAQBDIFSA-N SMILEShelp_outline C1[C@@]2([C@]3(CC[C@]4([C@]([C@@]3(CC=C2C[C@H](C1)O)[H])(CC[C@@]4([C@H](C)CCCC(C)C)[H])[H])C)[H])C 2D coordinates Mol file for the small molecule Search links Involved in 63 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline cholesteryl (7Z)-octadecenoate Identifier CHEBI:152049 Charge 0 Formula C45H78O2 InChIKeyhelp_outline MREOOHOCPSHRGR-AFFZRSIFSA-N SMILEShelp_outline O([C@@H]1CC=2[C@@](C3C(C4[C@@](C(CC4)[C@@H](CCCC(C)C)C)(CC3)C)CC2)(CC1)C)C(CCCCC/C=C\CCCCCCCCCC)=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CoA Identifier CHEBI:57287 (Beilstein: 11604429) help_outline Charge -4 Formula C21H32N7O16P3S InChIKeyhelp_outline RGJOEKWQDUBAIZ-IBOSZNHHSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 1,500 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:64328 | RHEA:64329 | RHEA:64330 | RHEA:64331 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Structural basis for catalysis and substrate specificity of human ACAT1.
Qian H., Zhao X., Yan R., Yao X., Gao S., Sun X., Du X., Yang H., Wong C.C.L., Yan N.
As members of the membrane-bound O-acyltransferase (MBOAT) enzyme family, acyl-coenzyme A:cholesterol acyltransferases (ACATs) catalyse the transfer of an acyl group from acyl-coenzyme A to cholesterol to generate cholesteryl ester, the primary form in which cholesterol is stored in cells and tran ... >> More
As members of the membrane-bound O-acyltransferase (MBOAT) enzyme family, acyl-coenzyme A:cholesterol acyltransferases (ACATs) catalyse the transfer of an acyl group from acyl-coenzyme A to cholesterol to generate cholesteryl ester, the primary form in which cholesterol is stored in cells and transported in plasma<sup>1</sup>. ACATs have gained attention as potential drug targets for the treatment of diseases such as atherosclerosis, Alzheimer's disease and cancer<sup>2-7</sup>. Here we present the cryo-electron microscopy structure of human ACAT1 as a dimer of dimers. Each protomer consists of nine transmembrane segments, which enclose a cytosolic tunnel and a transmembrane tunnel that converge at the predicted catalytic site. Evidence from structure-guided mutational analyses suggests that acyl-coenzyme A enters the active site through the cytosolic tunnel, whereas cholesterol may enter from the side through the transmembrane tunnel. This structural and biochemical characterization helps to rationalize the preference of ACAT1 for unsaturated acyl chains, and provides insight into the catalytic mechanism of enzymes within the MBOAT family<sup>8</sup>. << Less
Nature 581:333-338(2020) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.