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Gene Review

Lip1  -  Lipase 1

Drosophila melanogaster

Synonyms: CG7279, DmLip1, Dmel\CG7279, Dmlip1, LIP1Dm, ...
 
 
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Disease relevance of Lip1

 

High impact information on Lip1

 

Biological context of Lip1

  • These Drosophila lipases are related to acid lipases, with a common GHSQG motif, within a more general consensus GXSXG, identified as the active site shared by all the members of lipase superfamily [5].
  • We have used the yolk proteins as an outgroup to root a phylogeny of the lipase family [6].
  • Overall, the data suggests that CG3488 functions as a lipase and that analyses of its homologs will provide unique insights into lipid metabolism in many species [7].
  • The concentration dependence of lipase activity with TG and PL micellar substrates showed saturation kinetics, with apparent K(m) values of 152 +/- 11 and 7.8 +/- 1.1 muM, respectively [8].
  • They included protein-folding and stress-response proteins, a hormone, a lipase, a serpin, a cysteine-rich protein and two peptidases, a pro-enzyme form of a cathepsin K-like cysteine peptidase and a gamma-glutamyl transpeptidase [9].
 

Anatomical context of Lip1

 

Associations of Lip1 with chemical compounds

 

Other interactions of Lip1

  • Rolling blackout (RBO) is a putative transmembrane lipase required for phospholipase C-dependent phosphatidylinositol 4,5-bisphosphate-diacylglycerol signaling in Drosophila neurons [12].

References

  1. A lipase isolated from the silkworm Bombyx mori shows antiviral activity against nucleopolyhedrovirus. Ponnuvel, K.M., Nakazawa, H., Furukawa, S., Asaoka, A., Ishibashi, J., Tanaka, H., Yamakawa, M. J. Virol. (2003) [Pubmed]
  2. Rolling blackout, a newly identified PIP2-DAG pathway lipase required for Drosophila phototransduction. Huang, F.D., Matthies, H.J., Speese, S.D., Smith, M.A., Broadie, K. Nat. Neurosci. (2004) [Pubmed]
  3. Organization of the human lipoprotein lipase gene and evolution of the lipase gene family. Kirchgessner, T.G., Chuat, J.C., Heinzmann, C., Etienne, J., Guilhot, S., Svenson, K., Ameis, D., Pilon, C., d'Auriol, L., Andalibi, A. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  4. Cloning of a phosphatidic acid-preferring phospholipase A1 from bovine testis. Higgs, H.N., Han, M.H., Johnson, G.E., Glomset, J.A. J. Biol. Chem. (1998) [Pubmed]
  5. The Drosophila melanogaster lipase homologs: a gene family with tissue and developmental specific expression. Pistillo, D., Manzi, A., Tino, A., Boyl, P.P., Graziani, F., Malva, C. J. Mol. Biol. (1998) [Pubmed]
  6. Structure and evolution of the lipase superfamily. Hide, W.A., Chan, L., Li, W.H. J. Lipid Res. (1992) [Pubmed]
  7. Alpha/beta hydrolase2, a predicated gene adjacent to mad in Drosophila melanogaster, belongs to a new global multigene family and is associated with obesity. Wisotzkey, R.G., Johnson, A.N., Takaesu, N.T., Newfeld, S.J. J. Mol. Evol. (2003) [Pubmed]
  8. The main triglyceride-lipase from the insect fat body is an active phospholipase A1: identification and characterization. Arrese, E.L., Patel, R.T., Soulages, J.L. J. Lipid Res. (2006) [Pubmed]
  9. Proteomic identification of Drosophila melanogaster male accessory gland proteins, including a pro-cathepsin and a soluble gamma-glutamyl transpeptidase. Walker, M.J., Rylett, C.M., Keen, J.N., Audsley, N., Sajid, M., Shirras, A.D., Isaac, R.E. Proteome science [electronic resource]. (2006) [Pubmed]
  10. Brummer lipase is an evolutionary conserved fat storage regulator in Drosophila. Grönke, S., Mildner, A., Fellert, S., Tennagels, N., Petry, S., Müller, G., Jäckle, H., Kühnlein, R.P. Cell metabolism. (2005) [Pubmed]
  11. Purification and characterization of a novel lipase from the digestive glands of a primitive animal: the scorpion. Zouari, N., Miled, N., Cherif, S., Mejdoub, H., Gargouri, Y. Biochim. Biophys. Acta (2005) [Pubmed]
  12. Rolling blackout is required for synaptic vesicle exocytosis. Huang, F.D., Woodruff, E., Mohrmann, R., Broadie, K. J. Neurosci. (2006) [Pubmed]
 
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