Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline 1,2-di-(9Z-octadecenoyl)-sn-glycerol Identifier CHEBI:52333 (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 CTP Identifier CHEBI:37563 (Beilstein: 4732530) help_outline Charge -4 Formula C9H12N3O14P3 InChIKeyhelp_outline PCDQPRRSZKQHHS-XVFCMESISA-J SMILEShelp_outline Nc1ccn([C@@H]2O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]2O)c(=O)n1 2D coordinates Mol file for the small molecule Search links Involved in 82 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)-sn-glycero-3-phosphate Identifier CHEBI:74546 Charge -2 Formula C39H71O8P InChIKeyhelp_outline MHUWZNTUIIFHAS-DSSVUWSHSA-L SMILEShelp_outline CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@H](COP([O-])([O-])=O)OC(=O)CCCCCCC\C=C/CCCCCCCC 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CDP Identifier CHEBI:58069 Charge -3 Formula C9H12N3O11P2 InChIKeyhelp_outline ZWIADYZPOWUWEW-XVFCMESISA-K SMILEShelp_outline Nc1ccn([C@@H]2O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]2O)c(=O)n1 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 H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:43656 | RHEA:43657 | RHEA:43658 | RHEA:43659 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase.
Han G.-S., O'Hara L., Siniossoglou S., Carman G.M.
The Saccharomyces cerevisiae DGK1 gene encodes a diacylglycerol kinase enzyme that catalyzes the formation of phosphatidate from diacylglycerol. Unlike the diacylglycerol kinases from bacteria, plants, and animals, the yeast enzyme utilizes CTP, instead of ATP, as the phosphate donor in the reacti ... >> More
The Saccharomyces cerevisiae DGK1 gene encodes a diacylglycerol kinase enzyme that catalyzes the formation of phosphatidate from diacylglycerol. Unlike the diacylglycerol kinases from bacteria, plants, and animals, the yeast enzyme utilizes CTP, instead of ATP, as the phosphate donor in the reaction. Dgk1p contains a CTP transferase domain that is present in the SEC59-encoded dolichol kinase and CDS1-encoded CDP-diacylglycerol synthase enzymes. Deletion analysis showed that the CTP transferase domain was sufficient for diacylglycerol kinase activity. Point mutations (R76A, K77A, D177A, and G184A) of conserved residues within the CTP transferase domain caused a loss of diacylglycerol kinase activity. Analysis of DGK1 alleles showed that the in vivo functions of Dgk1p were specifically due to its diacylglycerol kinase activity. The DGK1-encoded enzyme had a pH optimum at 7.0-7.5, required Ca(2+) or Mg(2+) ions for activity, was potently inhibited by N-ethylmaleimide, and was labile at temperatures above 40 degrees C. The enzyme exhibited positive cooperative (Hill number = 2.5) kinetics with respect to diacylglycerol (apparent K(m) = 6.5 mol %) and saturation kinetics with respect to CTP (apparent K(m) = 0.3 mm). dCTP was both a substrate (apparent K(m) = 0.4 mm) and competitive inhibitor (apparent K(i) = 0.4 mm) of the enzyme. Diacylglycerol kinase activity was stimulated by major membrane phospholipids and was inhibited by CDP-diacylglycerol and sphingoid bases. << Less
J. Biol. Chem. 283:20443-20453(2008) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.