Enzymes
| UniProtKB help_outline | 1,598 proteins |
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- Name help_outline a monoacylglycerol Identifier CHEBI:17408 Charge 0 Formula C4H7O4R SMILEShelp_outline C(O*)C(O*)CO* 2D coordinates Mol file for the small molecule Search links Involved in 225 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,301 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a monoacyl-sn-glycero-3-phosphate Identifier CHEBI:77589 Charge -2 Formula C4H6O7PR SMILEShelp_outline [O-]P([O-])(=O)OC[C@@H](CO[*])O[*] 2D coordinates Mol file for the small molecule Search links Involved in 128 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) help_outline Charge -3 Formula C10H12N5O10P2 InChIKeyhelp_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 854 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 9,717 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:19293 | RHEA:19294 | RHEA:19295 | RHEA:19296 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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THE BIOSYNTHESIS OF PHOSPHATIDIC ACID AND LYSOPHOSPHATIDIC ACID BY GLYCERIDE PHOSPHOKINASE PATHWAYS IN ESCHERICHIA COLI.
PIERINGER R.A., KUNNES R.S.
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Biosynthesis of lysophosphatdic acid from monoglyceride and adenosine triphosphate.
PIERINGER R.A., HOKIN L.E.
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MuLK, a eukaryotic multi-substrate lipid kinase.
Waggoner D.W., Johnson L.B., Mann P.C., Morris V., Guastella J., Bajjalieh S.M.
We report the identification and characterization of a novel lipid kinase that phosphorylates multiple substrates. This enzyme, which we term MuLK for multi-substrate lipid kinase, does not belong to a previously described lipid kinase family. MuLK has orthologs in many organisms and is broadly ex ... >> More
We report the identification and characterization of a novel lipid kinase that phosphorylates multiple substrates. This enzyme, which we term MuLK for multi-substrate lipid kinase, does not belong to a previously described lipid kinase family. MuLK has orthologs in many organisms and is broadly expressed in human tissues. Although predicted to be a soluble protein, MuLK co-fractionates with membranes and localizes to an internal membrane compartment. Recombinant MuLK phosphorylates diacylglycerol, ceramide, and 1-acylglycerol but not sphingosine. Although its affinity for diacylglycerol and ceramide are similar, MuLK exhibits a higher V(max) toward diacylglycerol in vitro, consistent with it acting primarily as a diacylglycerol kinase. MuLK activity was inhibited by sphingosine and enhanced by cardiolipin. It was stimulated by calcium when magnesium concentrations were low and inhibited by calcium when magnesium concentrations were high. The effects of charged lipids and cations on MuLK activity in vitro suggest that its activity in vivo is tightly regulated by cellular conditions. << Less
J. Biol. Chem. 279:38228-38235(2004) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.