Phospholipase D: Difference between revisions

Revision as of 11:33, 5 October 2020

Function

Phospholipase D (PLD) hydrolyzes phosphatidylcholine (PC) into phosphatidic acid and choline^[1]. PLD is found in organisms ranging from virus to mammals.

Relevance

Dysregulation 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 highlights

The ^[3]. Water molecule are shown as red sphere.

Phospholipase D complex with substrate dibutyrylphosphatidylcholine (PDB code 1v0y)

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3D structures of phospholipase D3D structures of phospholipase D

Updated on 05-October-2020

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
1v0v, 1v0w – SaPLD + phosphite
1v0y – SaPLD + phosphatidylcholine derivative
2ze9 – SaPLD (mutant) + phosphatidylcholine
1v0t, 1v0u – SaPLD + glycerophosphate
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

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Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] 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

[2] 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

[3] 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

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@@ Line 15: / Line 15: @@
 Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+[[6u8z]] – hPLD1 catalytic domain 330-500, 643-1074 – human<br />
+[[6ohr]] – hPLD1 catalytic domain + inhibitor<br />
+[[6ohm]], [[6oho]] – hPLD2 catalytic domain 294-933<br />
+[[6ohq]], [[6ohs]], [[6ohp]] – hPLD2 catalytic domain + inhibitor<br />
 [[4rw3]] – bsPLD – brown spider<br />
 [[4rw5]] – bsPLD (mutant)<br />