Enzymes
| UniProtKB help_outline | 2,139 proteins |
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- Name help_outline 1,2-di-(9Z-octadecenoyl)-sn-glycerol Identifier CHEBI:52333 (Beilstein: 1730457; CAS: 24529-88-2) help_outline Charge 0 Formula C39H72O5 InChIKeyhelp_outline AFSHUZFNMVJNKX-LLWMBOQKSA-N SMILEShelp_outline CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@H](CO)OC(=O)CCCCCCC\C=C/CCCCCCCC 2D coordinates Mol file for the small molecule Search links Involved in 27 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline hexadecanoyl-CoA Identifier CHEBI:57379 Charge -4 Formula C37H62N7O17P3S InChIKeyhelp_outline MNBKLUUYKPBKDU-BBECNAHFSA-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(CCCCCCCCCCCCCCC)=O)=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 110 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol Identifier CHEBI:75583 Charge 0 Formula C55H102O6 InChIKeyhelp_outline JFISYPWOVQNHLS-HMOYFKASSA-N SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)OC[C@@H](COC(=O)CCCCCCC\C=C/CCCCCCCC)OC(=O)CCCCCCC\C=C/CCCCCCCC 2D coordinates Mol file for the small molecule Search links Involved in 4 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:38163 | RHEA:38164 | RHEA:38165 | RHEA:38166 | |
|---|---|---|---|---|
| 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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Synthesis of a novel acetylated neutral lipid related to platelet-activating factor by acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol acyltransferase in HL-60 cells.
Kawasaki T., Snyder F.
Acyl-CoA:1-O-hexadecyl-2-acetyl-sn-glycerol acyl-transferase, a newly detected enzyme related to platelet-activating factor metabolism, has been characterized in microsomes of a human leukemia cell line (HL-60 cells). It has a sharp pH optimum of 6.8, does not require divalent metal ions, is stabl ... >> More
Acyl-CoA:1-O-hexadecyl-2-acetyl-sn-glycerol acyl-transferase, a newly detected enzyme related to platelet-activating factor metabolism, has been characterized in microsomes of a human leukemia cell line (HL-60 cells). It has a sharp pH optimum of 6.8, does not require divalent metal ions, is stable at preincubation temperatures up to 45 degrees C, and among a variety of acyl-CoA thioesters (8:0-20:4) tested, linoleoyl-CoA is the best substrate. Km and Vmax values for 1-O-hexadecyl-2-acetyl-sn-glycerol acyltransferase are 8.5 microM and 1.7 nmol/min/mg of protein, respectively. For comparative purposes acyl-CoA:1,2-dioleoyl-sn-glycerol acyltransferase was also characterized in HL-60 microsomes. It has a relatively broad pH optimum of 6.1, is stimulated 1.4-fold by Mg2+, is relatively labile at preincubation temperatures higher than 25 degrees C, and among the various acyl-CoA thioesters tested, myristoyl-CoA is the best substrate. In substrate competition experiments, we found 1-O-hexadecyl-2-oleoyl-sn-glycerol is a competitive inhibitor (Ki = 32 microM). Our findings indicate acyl-CoA:1-O-hexadecyl-2-acetyl-sn-glycerol acyltransferase in HL-60 cells is distinctly different from acyl-CoA:1,2-dioleoyl-sn-glycerol acyltransferase. Our experimental results demonstrate that the unique enzyme activity characterized in this report also is expressed in intact HL-60 cells. << Less
J Biol Chem 263:2593-2596(1988) [PubMed] [EuropePMC]
This publication is cited by 14 other entries.
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The triacylglycerol synthesis enzyme DGAT1 also catalyzes the synthesis of diacylglycerols, waxes, and retinyl esters.
Yen C.L., Monetti M., Burri B.J., Farese R.V. Jr.
The final step of triacylglycerol biosynthesis is catalyzed by acyl CoA:diacylglycerol acyltransferase (DGAT) enzymes. The two known DGATs, DGAT1 and DGAT2, are encoded by unrelated genes. Although both DGAT1 and DGAT2 knockout mice have reduced tissue triacylglycerol contents, they have disparate ... >> More
The final step of triacylglycerol biosynthesis is catalyzed by acyl CoA:diacylglycerol acyltransferase (DGAT) enzymes. The two known DGATs, DGAT1 and DGAT2, are encoded by unrelated genes. Although both DGAT1 and DGAT2 knockout mice have reduced tissue triacylglycerol contents, they have disparate phenotypes, prompting us to investigate whether the two enzymes have unrecognized functional differences. We now report that DGAT1 exhibits additional acyltransferase activities in vitro, including those of acyl CoA:monoacylglycerol acyltransferase (MGAT), wax monoester and wax diester synthases, and acyl CoA:retinol acyltransferase (ARAT), which catalyze the synthesis of diacylglycerols, wax esters, and retinyl esters, respectively. These activities were demonstrated in in vitro assays with membranes from insect cells or homogenates from COS7 cells overexpressing DGAT1. Wax synthase and ARAT activities were also demonstrated in intact COS7 cells expressing DGAT1. Additionally, cells and tissues from DGAT1-deficient mice exhibited reduced ARAT activity, and the mice had increased levels of unesterified retinol in their livers on a high-retinol diet. Our findings indicate that DGAT1 can utilize a variety of acyl acceptors as substrates in vitro and suggest that these activities may be relevant to the in vivo functions of DGAT1. << Less
J. Lipid Res. 46:1502-1511(2005) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters.
Yen C.-L.E., Brown C.H. IV, Monetti M., Farese R.V. Jr.
Acyl-CoA-dependent O-acyltransferases catalyze reactions in which fatty acyl-CoAs are joined to acyl acceptors containing free hydroxyl groups to produce neutral lipids. In this report, we characterize a human multifunctional O-acyltransferase (designated MFAT) that belongs to the acyl-CoA:diacylg ... >> More
Acyl-CoA-dependent O-acyltransferases catalyze reactions in which fatty acyl-CoAs are joined to acyl acceptors containing free hydroxyl groups to produce neutral lipids. In this report, we characterize a human multifunctional O-acyltransferase (designated MFAT) that belongs to the acyl-CoA:diacylglycerol acyltransferase 2/acyl-CoA:monoacylglycerol acyltransferase (MGAT) gene family and is highly expressed in the skin. Membranes of insect cells and homogenates of mammalian cells overexpressing MFAT exhibited significantly increased MGAT, acyl-CoA:fatty acyl alcohol acyltransferase (wax synthase), and acyl-CoA:retinol acyltransferase (ARAT) activities, which catalyze the synthesis of diacylglycerols, wax monoesters, and retinyl esters, respectively. Furthermore, when provided with the appropriate substrates, intact mammalian cells overexpressing MFAT accumulated more waxes and retinyl esters than control cells. We conclude that MFAT is a multifunctional acyltransferase that likely plays an important role in lipid metabolism in human skin. << Less
J. Lipid Res. 46:2388-2397(2005) [PubMed] [EuropePMC]
This publication is cited by 7 other entries.