Enzymes
| UniProtKB help_outline | 1 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 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphoethanolamine Identifier CHEBI:78813 Charge 0 Formula C39H76NO8P InChIKeyhelp_outline DVXMEPWDARXHCX-OTMQOFQLSA-N SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC\C=C/CCCCCCCC)COP([O-])(=O)OCC[NH3+] 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 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 1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine Identifier CHEBI:74971 Charge 0 Formula C23H46NO7P InChIKeyhelp_outline PYVRVRFVLRNJLY-MZMPXXGTSA-N SMILEShelp_outline CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](O)COP([O-])(=O)OCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:44248 | RHEA:44249 | RHEA:44250 | RHEA:44251 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Saccharomyces cerevisiae phospholipid:diacylglycerol acyl transferase (PDAT) devoid of its membrane anchor region is a soluble and active enzyme retaining its substrate specificities.
Ghosal A., Banas A., Staahl U., Dahlqvist A., Lindqvist Y., Stymne S.
A N-terminal deleted version of the Saccharomyces cerevisiae phospholipid:diacylglycerol acyltransferase (ScPDAT), lacking the predicted membrane-spanning region, was fused in frame with alpha-factor secretion signal and expressed in Pichia pastoris under the control of the methanol inducible alco ... >> More
A N-terminal deleted version of the Saccharomyces cerevisiae phospholipid:diacylglycerol acyltransferase (ScPDAT), lacking the predicted membrane-spanning region, was fused in frame with alpha-factor secretion signal and expressed in Pichia pastoris under the control of the methanol inducible alcohol oxidase promoter. This resulted in a truncated, soluble and highly active PDAT protein secreted into the culture medium of the recombinant cells. The soluble as well as native membrane bound enzymes was shown to be glycosylated and extensive deglycosylation severely lowered the activity. The production of a soluble and extracellular PDAT allowed us to investigate substrate preferences of the enzyme without interference of endogenous lipids and enzymes. Similar to the membrane bound counterpart, the highest activity was achieved with acyl groups at sn-2 position of phosphatidylethanolamine as acyl donor and 1,2-diacylglycerols as acyl acceptor. The soluble enzyme was also able to catalyze, at a low rate, a number of transacylation reactions between various neutral lipids and between polar lipids and neutral lipids others than diacylglycerols, including acylation of long chain alcohols. << Less
Biochim. Biophys. Acta 1771:1457-1463(2007) [PubMed] [EuropePMC]
This publication is cited by 14 other entries.