Enzymes
| UniProtKB help_outline | 182 proteins |
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- Name help_outline a 2-acylglycerol Identifier CHEBI:17389 Charge 0 Formula C4H7O4R SMILEShelp_outline OCC(CO)OC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 71 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1,2-diacyl-sn-glycero-3-phosphocholine Identifier CHEBI:57643 Charge 0 Formula C10H18NO8PR2 SMILEShelp_outline [C@](COC(=O)*)(OC(=O)*)([H])COP(OCC[N+](C)(C)C)([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 325 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1,2-diacylglycerol Identifier CHEBI:49172 Charge 0 Formula C5H6O5R2 SMILEShelp_outline OCC(COC([*])=O)OC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 296 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1-acyl-sn-glycero-3-phosphocholine Identifier CHEBI:58168 Charge 0 Formula C9H19NO7PR SMILEShelp_outline C[N+](C)(C)CCOP([O-])(=O)OC[C@H](O)COC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 218 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:78439 | RHEA:78440 | RHEA:78441 | RHEA:78442 | |
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| 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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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.