N-acetylphosphatidylethanolamine-hydrolysing phospholipase D

Enzyme involved in biosynthesis of anandamide

Identifiers

EC no.

3.1.4.54

Databases

IntEnz

IntEnz view

BRENDA

BRENDA entry

ExPASy

NiceZyme view

KEGG

KEGG entry

MetaCyc

metabolic pathway

PRIAM

profile

PDB structures

RCSB PDB PDBe PDBsum

Search
PMC	articles
PubMed	articles
NCBI	proteins

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.^[1]^[2] 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.

References

^ Okamoto Y, Morishita J, Tsuboi K, Tonai T, Ueda N (February 2004). "Molecular characterization of a phospholipase D generating anandamide and its congeners". The Journal of Biological Chemistry. 279 (7): 5298–305. doi:10.1074/jbc.M306642200. PMID 14634025.
^ Wang J, Okamoto Y, Morishita J, Tsuboi K, Miyatake A, Ueda N (May 2006). "Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-β-lactamase family". The Journal of Biological Chemistry. 281 (18): 12325–35. doi:10.1074/jbc.M512359200. PMID 16527816.

Magotti, Paola; Bauer, Inga; Igarashi, Miki; Babagoli, Masih; Marotta, Roberto; Piomelli, Daniele; Garau, Gianpiero (March 2015). "Structure of Human N-Acylphosphatidylethanolamine-Hydrolyzing Phospholipase D: Regulation of Fatty Acid Ethanolamide Biosynthesis by Bile Acids". Structure. 23 (3): 598–604. doi:10.1016/j.str.2014.12.018. PMC 4351732. PMID 25684574.

External links

N-acetylphosphatidylethanolamine-hydrolysing+phospholipase+D at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
N-acyl phosphatidylethanolamine phospholipase D (NAPEPLD ((C7orf18, FMP30, NAPE-PLD)) Human Protein Atlas

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4:
Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease
and ribonuclease)

3.1.11-16:
Exonuclease

Exodeoxyribonuclease	RecBCD
Exoribonuclease	Oligonucleotidase

3.1.21-31:
Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme;see {{Restriction enzyme}} UvrABC endonuclease
Endoribonuclease	RNase III Drosha: Microprocessor complex Dicer: RNA-induced silencing complex RNase H 1 2A 2B 2C RNase P RNase A RNase Z RNase E 1 2 3 4/5 RNase T1
either deoxy- or ribo-	Nuclease S1 Mung bean nuclease Serratia marcescens nuclease Micrococcal nuclease

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)