:N-acetylphosphatidylethanolamine-hydrolysing phospholipase D

{{short description|Enzyme involved in biosynthesis of anandamide}}

{{Infobox enzyme

| Name = N-acetylphosphatidylethanolamine-hydrolysing phospholipase D

| EC_number = 3.1.4.54

| CAS_number =

| GO_code =

| image =

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| caption =

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N-acetylphosphatidylethanolamine-hydrolysing phospholipase D (EC 3.1.4.54, NAPE-PLD, anandamide-generating phospholipase D, N-acyl phosphatidylethanolamine phospholipase D, NAPE-hydrolyzing phospholipase D) is an enzyme with systematic name N-acetylphosphatidylethanolamine phosphatidohydrolase.{{cite journal | vauthors = Okamoto Y, Morishita J, Tsuboi K, Tonai T, Ueda N | title = Molecular characterization of a phospholipase D generating anandamide and its congeners | journal = The Journal of Biological Chemistry | volume = 279 | issue = 7 | pages = 5298–305 | date = February 2004 | pmid = 14634025 | doi = 10.1074/jbc.M306642200 | doi-access = free }}{{cite journal | vauthors = Wang J, Okamoto Y, Morishita J, Tsuboi K, Miyatake A, Ueda N | title = Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-β-lactamase family | journal = The Journal of Biological Chemistry | volume = 281 | issue = 18 | pages = 12325–35 | date = May 2006 | pmid = 16527816 | doi = 10.1074/jbc.M512359200 | doi-access = free }} It catalyses the following chemical reaction

: N-acylphosphatidylethanolamine + H2O \rightleftharpoons N-acylethanolamine + a 1,2-diacylglycerol 3-phosphate

This enzyme is involved in the biosynthesis of anandamide.

See also

References

{{reflist}}

  • {{cite journal |last1=Magotti |first1=Paola |last2=Bauer |first2=Inga |last3=Igarashi |first3=Miki |last4=Babagoli |first4=Masih |last5=Marotta |first5=Roberto |last6=Piomelli |first6=Daniele |last7=Garau |first7=Gianpiero |title=Structure of Human N-Acylphosphatidylethanolamine-Hydrolyzing Phospholipase D: Regulation of Fatty Acid Ethanolamide Biosynthesis by Bile Acids |journal=Structure |date=March 2015 |volume=23 |issue=3 |pages=598–604 |doi=10.1016/j.str.2014.12.018 |pmid=25684574 |pmc=4351732}}