Phospholipase D

Phospholipase D
Identifiers
SymbolPLDc
PfamPF03009
InterProIPR001736
SMARTSM00155
PROSITEPDOC50035
SCOP21byr / SCOPe / SUPFAM
OPM superfamily118
OPM protein3rlh
CDDcd00138
Membranome306
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
phospholipase D
Identifiers
EC no.3.1.4.4
CAS no.9001-87-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Phospholipase D (EC 3.1.4.4, lipophosphodiesterase II, lecithinase D, choline phosphatase, PLD; systematic name phosphatidylcholine phosphatidohydrolase) is an enzyme of the phospholipase superfamily that catalyses the following reaction

a phosphatidylcholine + H2O = choline + a phosphatidate

Phospholipases occur widely, and can be found in a wide range of organisms, including bacteria, yeast, plants, animals, and viruses.[1][2] Phospholipase D's principal substrate is phosphatidylcholine, which it hydrolyzes to produce the signal molecule phosphatidic acid (PA), and soluble choline in a cholesterol dependent process called substrate presentation.[3] Plants contain numerous genes that encode various PLD isoenzymes, with molecular weights ranging from 90 to 125 kDa.[4] Mammalian cells encode two isoforms of phospholipase D: PLD1 and PLD2.[5] Phospholipase D is an important player in many physiological processes, including membrane trafficking, cytoskeletal reorganization, receptor-mediated endocytosis, exocytosis, and cell migration.[6] Through these processes, it has been further implicated in the pathophysiology of multiple diseases: in particular the progression of Parkinson's and Alzheimer's, as well as various cancers.[4][6] PLD may also help set the threshold for sensitivity to anesthesia and mechanical force.[7][8]

  1. ^ Jenkins GM, Frohman MA (October 2005). "Phospholipase D: a lipid centric review". Cellular and Molecular Life Sciences. 62 (19–20): 2305–16. doi:10.1007/s00018-005-5195-z. PMC 11139095. PMID 16143829. S2CID 26447185.
  2. ^ Exton JH (2002). "Phospholipase D-structure, regulation and function". Reviews of Physiology, Biochemistry and Pharmacology. 144: 1–94. doi:10.1007/BFb0116585. ISBN 978-3-540-42814-5. PMID 11987824.
  3. ^ Petersen EN, Chung HW, Nayebosadri A, Hansen SB (December 2016). "Kinetic disruption of lipid rafts is a mechanosensor for phospholipase D". Nature Communications. 7 (1): 13873. Bibcode:2016NatCo...713873P. doi:10.1038/ncomms13873. PMC 5171650. PMID 27976674.
  4. ^ a b Kolesnikov YS, Nokhrina KP, Kretynin SV, Volotovski ID, Martinec J, Romanov GA, Kravets VS (January 2012). "Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells". Biochemistry. Biokhimiia. 77 (1): 1–14. doi:10.1134/S0006297912010014. PMID 22339628. S2CID 14815405.
  5. ^ Peng X, Frohman MA (February 2012). "Mammalian phospholipase D physiological and pathological roles". Acta Physiologica. 204 (2): 219–26. doi:10.1111/j.1748-1716.2011.02298.x. PMC 3137737. PMID 21447092.
  6. ^ a b Foster DA, Xu L (September 2003). "Phospholipase D in cell proliferation and cancer". Molecular Cancer Research. 1 (11): 789–800. PMID 14517341.
  7. ^ Petersen EN, Gudheti M, Pavel MA, Murphy KR, William WJ, Jorgensen EM, Hansen SB (5 September 2019). "Phospholipase D Transduces Force to TREK-1 Channels in a Biological Membrane". bioRxiv: 758896. doi:10.1101/758896.
  8. ^ Pavel MA, Petersen EN, Wang H, Lerner RA, Hansen SB (June 2020). "Studies on the mechanism of general anesthesia". Proceedings of the National Academy of Sciences of the United States of America. 117 (24): 13757–13766. Bibcode:2020PNAS..11713757P. bioRxiv 10.1101/313973. doi:10.1073/pnas.2004259117. PMC 7306821. PMID 32467161.