Substrate chirality and specificity of diacylglycerol kinases and the multisubstrate lipid kinase

Biochemistry

Volumn 46, Issue 49, 2007, Pages 14225-14231

  Epand, Richard M ^a   Shulga, Yulia V ^a   Timmons, Heath C ^b   Perri, Alexandra L ^a   Belani, Jitendra D ^b   Perinpanathan, Kirishanth ^a   Johnson McIntire, Laura Beth ^c   Bajjalieh, Sandra ^c   Dicu, Armela O ^a   Elias, Cynthia ^d   Rychnovsky, Scott D ^b   Topham, Matthew K ^e  

^a MCMASTER UNIVERSITY   (Canada)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^d NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^e UNIVERSITY OF UTAH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; DIACYLGLYCEROL KINASE; SUBSTRATE BINDING;

BIOCHEMISTRY; CHIRALITY; LIPIDS; PHOSPHORYLATION; SUBSTRATES;

ENZYMES;

2,3 DIOLEOYLGLYCEROL; DIACYLGLYCEROL KINASE; GLYCEROL 1,2 DIOLEATE; UNCLASSIFIED DRUG;

ARTICLE; CHIRALITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME KINETICS; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; PRIORITY JOURNAL; STEREOSPECIFICITY;

BINDING SITES; DIACYLGLYCEROL KINASE; DIGLYCERIDES; HUMANS; KINETICS; LIPOPROTEIN LIPASE; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); STEREOISOMERISM; SUBSTRATE SPECIFICITY;

EID: 37149021094     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701584v     Document Type: Article

References (31)

1. Topham, M. K. (2006) Signaling roles of diacylglycerol kinases, J. Cell. Biochem. 97, 474-484.
2. Sakane, F., Imai, S., Kai, M., Yasuda, S., and Kanoh, H. (2007) Diacylglycerol kinases: Why so many of them? Biochim. Biophys. Acta 1771, 793-806.
3. Waggoner, D. W., Johnson, L. B., Mann, P. C., Morris, V., Guastella, J., and Bajjalieh, S. M. (2004) MuLK, a eukaryotic multi-substrate lipid kinase, J. Biol. Chem. 279, 38228-38235.
4. Bektas, M., Payne, S. G., Liu, H., Goparaju, S., Milstien, S., and Spiegel, S. (2005) A novel acylglycerol kinase that produces lysophosphatidic acid modulates cross talk with EGFR in prostate cancer cells, J. Cell Biol. 169, 801-811.
5. Gorzelle, B. M., Nagy, J. K., Oxenoid, K., Lonzer, W. L., Cafiso, D. S., and Sanders, C. R. (1999) Reconstitutive refolding of diacylglycerol kinase, an integral membrane protein, Biochemistry 38, 16373-16382.
6. de Chaffoy de Courcelles, D., Roevens, P., and Van Belle, H. (1985) R 59 022, a diacylglycerol kinase inhibitor. Its effect on diacylglycerol and thrombin-induced C kinase activation in the intact platelet, J. Biol. Chem. 260, 15762-15770.
7. de Chaffoy de Courcelles, D., Roevens, P., Van Belle, H., Kennis, L., Somers, Y., and De Clerck, F. (1989) The role of endogenously formed diacylglycerol in the propagation and termination of platelet activation. A biochemical and functional analysis using the novel diacylglycerol kinase inhibitor, R 59 949, J. Biol. Chem. 264, 3274-3285.
8. Jiang, Y., Sakane, F., Kanoh, H., and Walsh, J. P. (2000) Selectivity of the diacylglycerol kinase inhibitor 3-[2-(4-[bis-(4-fluorophenyl)methylene]-1- piperidinyl)ethyl]-2,3-dihydro-2-thioxo-4(1H)quinazolinone (R59949) among diacylglycerol kinase subtypes, Biochem. Pharmacol. 59, 763-772.
9. Gómez-Merino, F. C., Arana-Ceballos, F. A., Trejo-Téllez, L. I., Skirycz, A., Brearley, C. A., Dörmann, P., and Mueller-Roeber, B. (2005) Arabidopsis AtDGK7, the smallest member of plant diacylglycerol kinases (DGKs), displays unique biochemical features and saturates at low substrate concentration: The DGK inhibitor R59022 differentially affects AtDGK2 and AtDGK7 activity in vitro and alters plant growth and development, J. Biol. Chem. 280, 34888-34899.
10. 2+-dependent stimuli. Evidence for two separate but convergent pathways, Biochem. Pharmacol. 36, 3459-3462.
11. Gomez-Cambronero, J., Molski, T. F., Becker, E. L., and Sha'afi, R. I. (1987) The diacylglycerol kinase inhibitor R59022 potentiates superoxide production but not secretion induced by fMet-Leu-Phe: Effects of leupeptin and the protein kinase C inhibitor H-7, Biochem. Biophys. Res. Commun. 148, 38-46.
12. Alonso, R., Rodríguez, M. C., Pindado, J., Merino, E., Mérida, I., and Izquierdo, M. (2005) Diacylglycerol kinase α regulates the secretion of lethal exosomes bearing Fas ligand during activation-induced cell death of T lymphocytes, J. Biol. Chem. 280, 28439-28450.
13. Alonso, R., Mazzeo, C., Merida, I., and Izquierdo, M. (2007) A new role of diacylglycerol kinase α on the secretion of lethal exosomes bearing Fas ligand during activation-induced cell death of T lymphocytes, Biochimie 89, 213-221.
14. Batista, E. L., Jr., Warbington, M., Badwey, J. A., and Van Dyke, T. E. (2005) Differentiation of HL-60 cells to granulocytes involves regulation of select diacylglycerol kinases (DGKs), J. Cell. Biochem. 94, 774-793.
15. Bunting, M., Tang, W., Zimmerman, G. A., McIntyre, T. M., and Prescott, S. M. (1996) Molecular cloning and characterization of a novel human diacylglycerol kinase ζ, J. Biol. Chem. 271, 10230-10236.
16. Younes, A., Kahn, D. W., Besterman, J. M., Bittman, R., Byun, H. S., and Kolesnick, R. N. (1992) Ceramide is a competitive inhibitor of diacylglycerol kinase in vitro and in intact human leukemia (HL-60) cells, J. Biol. Chem. 267, 842-847.
17. Bakali, H. M. A., Herman, M. D., Johnson, K. A., Kelly, A. A., Wieslander, A., Hallberg, B. M., and Nordlund, P. (2007) Crystal Structure of YegS, a Homologue to the Mammalian Diacylglycerol Kinases, Reveals a Novel Regulatory Metal Binding Site, J. Biol. Chem. 282, 19644-19652.
18. Vilcheze, C., and Bittman, R. (1994) An efficient asymmetric synthesis of diacylglycerols, J. Lipid Res. 35, 734-738.
19. Schaus, S. E., Brandes, B. D., Larrow, J. F., Tokunaga, M., Hansen, K. B., Gould, A. E., Furrow, M. E., and Jacobsen, E. N. (2002) Highly selective hydrolytic kinetic resolution of terminal epoxides catalyzed by chiral (salen)Co(III) complexes. Practical synthesis of enantioenriched terminal epoxides and 1,2-diols, J. Am. Chem. Soc. 124, 1307-1315.
20. Ward, D. E., and Rhee, C. K. (1991) A Simple Method for the Microscale Preparation of Mosher Acid Chloride, Tetrahedron Lett. 32, 7165-7166.
21. Tom, R. L., Caron, A. W., Massie, B., and Kamen, A. A. (1995) Scale-up of recombinant virus and protein production in stirred-tank reactors, Methods Mol. Biol. 39, 203-224.
22. Walsh, J. P., Suen, R., Lemaitre, R. N., and Glomset, J. A. (1994) Arachidonoyl-diacylglycerol kinase from bovine testis. Purification and properties, J. Biol. Chem. 269, 21155-21164.
23. Thirugnanam, S., Topham, M. K., and Epand, R. M. (2001) Physiological implications of the contrasting modulation of the activities of the ε and ζ isoforms of diacylglycerol kinase, Biochemistry 40, 10607-10613.
24. Epand, R. M., Kam, A., Bridgelal, N., Saiga, A., and Topham, M. K. (2004) The α isoform of diacylglycerol kinase exhibits arachidonoyl specificity with alkylacylglycerol, Biochemistry 43, 14778-14783.
25. Sakane, F., Yamada, K., Imai, S., and Kanoh, H. (1991) Porcine 80-kDa diacylglycerol kinase is a calcium-binding and calcium/phospholipid-dependent enzyme and undergoes calcium-dependent translocation, J. Biol. Chem. 266, 7096-7100.
26. Johnson, J. E., Zimmerman, M. L., Daleke, D. L., and Newton, A. C. (1998) Lipid structure and not membrane structure is the major determinant in the regulation of protein kinase C by phosphatidylserine, Biochemistry 37, 12020-12025.
27. Kates, M., Moldoveanu, N., and Stewart, L. C. (1993) On the revised structure of the major phospholipid of Halobacterium salinarium, Biochim. Biophys. Acta 1169, 46-53.
28. Sakane, F., Kai, M., Wada, I., Imai, S., and Kanoh, H. (1996) The C-terminal part of diacylglycerol kinase α lacking zinc fingers serves as a catalytic domain, Biochem. J. 318 (Part 2), 583-590.
29. Fernandez-Lorente, G., Fernandez-Lafuente, R., Palomo, J. M., Mateo, C., Bastida, A., Coca, J., Haramboure, T., Hernandez-Justiz, O., Terreni, M., and Guisan, J. M. (2001) Biocatalyst engineering exerts a dramatic effect on selectivity of hydrolysis catalyzed by immobilized lipases in aqueous medium, J. Mol. Catal. B: Enzym. 11, 649-656.
30. Sabbani, S., Hedenstrom, E., and Nordin, O. (2006) The enantioselectivity of Candida rugosa lipase is influenced by the particle size of the immobilising support material Accurel, J. Mol. Catal. B: Enzym. 42, 1-9.
31. Palomo, J. M., Segura, R. L., Fernandez-Lorente, G., Fernandez-Lafuente, R., and Guisan, J. M. (2007) Glutaraldehyde modification of lipases adsorbed on aminated supports: A simple way to improve their behaviour as enantioselective biocatalyst, Enzyme Microb. Technol. 40, 704-707.