Class of enzymes
Phospholipase D (EC 3.1.4.4, lipophosphodiesterase II, lecithinase D, choline phosphatase, PLD ; systematic name phosphatidylcholine phosphatidohydrolase ) is an anesthetic sensitive[ 1] [ 2] enzyme of the phospholipase superfamily that catalyses the following reaction
a phosphatidylcholine + H2 O = choline + a phosphatidate Phospholipases occur widely, and can be found in a wide range of organisms, including bacteria, yeast, plants, animals, and viruses.[ 3] [ 4] 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 .[ 5] isoenzymes , with molecular weights ranging from 90 to 125 kDa .[ 6] PLD1 and PLD2 .[ 7] physiological processes, including membrane trafficking , cytoskeletal reorganization, receptor-mediated endocytosis , exocytosis , and cell migration .[ 8] pathophysiology of multiple diseases : in particular the progression of Parkinson's and Alzheimer's , as well as various cancers .[ 6] [ 8] [ 9] [ 10]
^ Pavel, Mahmud Arif; Petersen, E. Nicholas; Wang, Hao; Lerner, Richard A.; Hansen, Scott B. (16 June 2020). "Studies on the mechanism of general anesthesia" . Proceedings of the National Academy of Sciences . 117 (24): 13757–13766. Bibcode :2020PNAS..11713757P . doi :10.1073/pnas.2004259117 PMC 7306821 ^ Petersen, E. Nicholas; Chung, Hae-Won; Nayebosadri, Arman; Hansen, Scott B. (15 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 . ^ 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 . ^ 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 . ^ 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 . ^ 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 . ^ 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 . ^ a b Foster DA, Xu L (September 2003). "Phospholipase D in cell proliferation and cancer". Molecular Cancer Research . 1 (11): 789–800. PMID 14517341 . ^ 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 ^ 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 .