Phospholipase D
FunctionPhospholipase D (PLD) hydrolyzes phosphatidylcholine (PC) into phosphatidic acid and choline[1]. PLD is found in organisms ranging from virus to mammals. RelevanceDysregulation of lipid pathways is involved in many neurodegenerative disorders like Alzheimer disease. Brains of Alzheimer disease patients show decreased levels of PC and increased activity of PLD[2]. Structural highlightsThe [3]. Water molecule are shown as red sphere. 3D structures of phospholipase D
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3D structures of phospholipase D3D structures of phospholipase D
Updated on 28-August-2023
6u8z – hPLD1 catalytic domain 330-500, 643-1074 – human
6ohr – hPLD1 catalytic domain + inhibitor
6ohm, 6oho – hPLD2 catalytic domain 294-933
6ohq, 6ohs, 6ohp – hPLD2 catalytic domain + inhibitor
4rw3 – bsPLD – brown spider
4rw5 – bsPLD (mutant)
3rlg, 3rlh – PLD (mutant) – Loxosceles intemedia
4q6x – PLD – cave spider
2ze4, 1v0r, 1v0s, 1f0i – SaPLD – Streptomyces antibioticus
7jrb – SaPLD (mutant)
1v0v, 1v0w – SaPLD + phosphite
1v0y – SaPLD + phosphatidylcholine derivative
2ze9 – SaPLD (mutant) + phosphatidylcholine
1v0t, 1v0u – SaPLD + glycerophosphate
7jrc – SaPLD (mutant) + phosphate
7js5, 7js7 – SaPLD (mutant) + inositol phosphate
7jru, 7jrv, 7jrw – SaPLD (mutant) + phosphatidic acid
6kz9 – AtPLD a 1 – Arabidopsis thaliana
6kz8 – AtPLD a 1 + phosphatidic acid
ReferencesReferences
- ↑ McDermott M, Wakelam MJ, Morris AJ. Phospholipase D. Biochem Cell Biol. 2004 Feb;82(1):225-53. PMID:15052340 doi:http://dx.doi.org/10.1139/o03-079
- ↑ Oliveira TG, Di Paolo G. Phospholipase D in brain function and Alzheimer's disease. Biochim Biophys Acta. 2010 Aug;1801(8):799-805. doi:, 10.1016/j.bbalip.2010.04.004. Epub 2010 Apr 23. PMID:20399893 doi:http://dx.doi.org/10.1016/j.bbalip.2010.04.004
- ↑ Leiros I, McSweeney S, Hough E. The reaction mechanism of phospholipase D from Streptomyces sp. strain PMF. Snapshots along the reaction pathway reveal a pentacoordinate reaction intermediate and an unexpected final product. J Mol Biol. 2004 Jun 11;339(4):805-20. PMID:15165852 doi:http://dx.doi.org/10.1016/j.jmb.2004.04.003