Literature summary for 3.1.4.54 extracted from

Magotti, P.; Bauer, I.; Igarashi, M.; Babagoli, M.; Marotta, R.; Piomelli, D.; Garau, G.
Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D regulation of fatty acid ethanolamide biosynthesis by bile acids (2015), Structure, 23, 598-604 .

Activating Compound

Activating Compound	Comment	Organism	Structure
deoxycholate	presence of deoxycholate stabilizes the enzyme dimer and increases the catalytic activity with EC50 value of 0.186 mM. Binding is rapid and reversible	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.65 A resolution. NAPE-PLD forms homodimers partly separated by an internal about 9 A wide channel and adapted to associate with phospholipids. A hydrophobic cavity provides an entryway for N-acylphosphatidylethanolamine into the active site, where a binuclear Zn2+ center is involved in hydrolysis. Bile acids bind with high affinity to selective pockets in this cavity, enhancing dimer assembly and enabling catalysis	Homo sapiens

Crystallization (Comment)

Organism

to 2.65 A resolution. NAPE-PLD forms homodimers partly separated by an internal about 9 A wide channel and adapted to associate with phospholipids. A hydrophobic cavity provides an entryway for N-acylphosphatidylethanolamine into the active site, where a binuclear Zn2+ center is involved in hydrolysis. Bile acids bind with high affinity to selective pockets in this cavity, enhancing dimer assembly and enabling catalysis

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
Q158S/Y159S	mutant is unable to form stable dimers and shows a decreased melting temperature	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	associated to membrane. At the membrane interface, the NAPE-PLD dimer forms a hydrophobic nook that contains two molecules of phosphatidylethanolamine, one bound to each monomer	Homo sapiens	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	a binuclear Zn2+ center is involved in hydrolysis	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q6IQ20	-	-

Synonyms

Synonyms	Comment	Organism
NAPEPLD	-	Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
70	-	melting temperature, mutant Q158S/Y159S	Homo sapiens
77	-	melting temperature, wild-type	Homo sapiens