Enzymes
UniProtKB help_outline | 443 proteins |
Reaction participants Show >> << Hide
- Name help_outline (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA Identifier CHEBI:57368 Charge -4 Formula C41H62N7O17P3S InChIKeyhelp_outline JDEPVTUUCBFJIW-YQVDHACTSA-J SMILEShelp_outline CCCCC\C=C/C\C=C/C\C=C/C\C=C/CCCC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(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 2D coordinates Mol file for the small molecule Search links Involved in 44 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 (5Z,8Z,11Z,14Z)-eicosatetraenoate Identifier CHEBI:82751 (CAS: 604-34-2) help_outline Charge 0 Formula C47H76O2 InChIKeyhelp_outline IMXSFYNMSOULQS-BEDFLICRSA-N SMILEShelp_outline CCCCC\C=C/C\C=C/C\C=C/C\C=C/CCCC(=O)O[C@H]1CC[C@]2(C)[C@H]3CC[C@]4(C)[C@H](CC[C@H]4[C@@H]3CC=C2C1)[C@H](C)CCCC(C)C 2D coordinates Mol file for the small molecule Search links Involved in 2 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:42816 | RHEA:42817 | RHEA:42818 | RHEA:42819 | |
---|---|---|---|---|
Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
|
Related reactions help_outline
More general form(s) of this reaction
Publications
-
Differential modulation of ACAT1 and ACAT2 transcription and activity by long chain free fatty acids in cultured cells.
Seo T., Oelkers P.M., Giattina M.R., Worgall T.S., Sturley S.L., Deckelbaum R.J.
Fatty acyl CoA and cholesterol are the substrates for cholesteryl ester synthesis by acyl coenzyme A:cholesterol acyltransferase (ACAT). Two ACAT genes have been identified; ACAT1 is expressed ubiquitously while ACAT2 is primarily expressed in intestine and liver. We tested effects of different fr ... >> More
Fatty acyl CoA and cholesterol are the substrates for cholesteryl ester synthesis by acyl coenzyme A:cholesterol acyltransferase (ACAT). Two ACAT genes have been identified; ACAT1 is expressed ubiquitously while ACAT2 is primarily expressed in intestine and liver. We tested effects of different free fatty acids (FFAs) on ACAT1 and ACAT2 expression and activity in HepG2 human hepatocytes and THP1 human macrophages. Incubation of oleic acid, arachidonic acid, or eicosapentaenoic acid, but not 25-hydroxycholesterol, induced ACAT1 mRNA levels 1.5--2-fold in HepG2, with no affect on ACAT2 mRNA. FFA had no affect on ACAT1 mRNA in THP1 cells. To determine if FFAs affect ACAT1 or ACAT2 posttranscriptionally, cells were labeled with [(3)H]cholesterol in the presence of the different FFAs for 1--5 h. Both HepG2 and THP1 cells showed the greatest cholesteryl ester production with oleic acid. This was also confirmed by the observation that more [(3)H]oleic acid incorporated into CE compared to [(3)H]eicosapentaenoic acid, even though there was no difference in the total uptake of these FFAs. In ACAT-deficient SRD4, CHO cells stably transfected with human ACAT1 or ACAT2, ACAT1 expressing cells showed a strong preference for oleic acid while ACAT2 expressing cells utilized unsaturated FFAs. Acyl CoA substrate specificity was further tested in microsomes isolated from these cells as well as HepG2 and THP1. THP1 and ACAT1 cells utilized oleoyl CoA preferentially. In contrast, HepG2 and ACAT2 microsomes utilized linolenoyl CoA as well. We conclude that FFAs increase ACAT1 mRNA levels in a cell specific manner, and furthermore that the ACAT reactions exhibit differential FFA utilization. << Less
Biochemistry 40:4756-4762(2001) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
-
Functional expression of a cDNA to human acyl-coenzyme A:cholesterol acyltransferase in yeast. Species-dependent substrate specificity and inhibitor sensitivity.
Yang H., Cromley D., Wang H., Billheimer J.T., Sturley S.L.
We have identified two yeast genes with similarity to a human cDNA encoding acyl-coenzyme A:cholesterol acyltransferase (ACAT). Deletion of both yeast genes results in a viable cell with undetectable esterified sterol (Yang, H., Bard, M., Bruner, D. A., Gleeson, A., Deckelbaum, R. J., Aljinovic, G ... >> More
We have identified two yeast genes with similarity to a human cDNA encoding acyl-coenzyme A:cholesterol acyltransferase (ACAT). Deletion of both yeast genes results in a viable cell with undetectable esterified sterol (Yang, H., Bard, M., Bruner, D. A., Gleeson, A., Deckelbaum, R. J., Aljinovic, G., Pohl, T., Rothstein, R., and Sturley, S. L. (1996) Science 272, 1353-1356). Here, we expressed the human cDNA in the yeast double mutant, resulting in high level production of ACAT protein, but low in vivo esterification of ergosterol, the predominant yeast sterol. The activity of the human enzyme was increased by incubation of these cells with 25-hydroxy, cholesterol, an established positive regulator of mammalian sterol esterification. In contrast, the yeast enzymes were unaffected by this reagent. In vitro microsomal assays indicated no sterol esterification in extracts from the double mutant. However, significant activity was detected from strains expressing human ACAT when cholesterol was equilibrated with the microsomal membranes. The human enzyme in yeast utilized cholesterol as the preferred sterol and was sensitive to competitive (S58035) and non-competitive (DuP 128) ACAT inhibitors. The yeast esterifying enzymes exhibited a diminished sterol substrate preference and were sensitive only to S58035. Human ACAT had a broad acyl-CoA substrate specificity, the other substrate for this reaction. By contrast, the yeast enzymes had a marked preference for specific acyl-CoAs, particularly unsaturated C18 forms. These results confirm the yeast genes as functional homologs of the human gene and demonstrate that the enzymes confer substrate specificity to the esterification reaction in both organisms. << Less
J. Biol. Chem. 272:3980-3985(1997) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.