3.1.4.54: N-acetylphosphatidylethanolamine-hydrolysing phospholipase D

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For detailed information about N-acetylphosphatidylethanolamine-hydrolysing phospholipase D, go to the full flat file.

Reaction

Synonyms

anandamide-generating phospholipase D, N-acyl phosphatidylethanolamine phospholipase D, N-acyl-phosphatidylethanolamine-specific phospholipase D, N-acylphosphatidylethanolamine-specific phospholipase D, NAPE-hydrolysing phospholipase D, NAPE-PLD, NAPEPLD

ECTree

     3 Hydrolases

         3.1 Acting on ester bonds

             3.1.4 Phosphoric-diester hydrolases

                3.1.4.54 N-acetylphosphatidylethanolamine-hydrolysing phospholipase D

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21	Activating Compound
726	AA Sequence
4	Application
12	Cloned(Commentary)
1	Crystallization (Commentary)
36	Disease/ Diagnostics
5	Expression
22	General Information
3	General Stability
5	IC50 Value
32	Inhibitors
32	KM Value [mM]
6	Localization
29	Metals/Ions
6	Molecular Weight [Da]
14	Natural Substrates/ Products (Substrates)
321	Organism
3	Pathway
2	PDB ID
10	pH Optimum
3	Posttranslational Modification
38	Protein Variants
6	Purification (Commentary)
1	Reaction
43	Reference
51	Source Tissue
6	Specific Activity [micromol/min/mg]
1	Storage Stability
64	Substrates and Products (Substrate)
6	Subunits
31	Synonyms
1	Systematic Name
9	Temperature Optimum [°C]
2	Temperature Stability [°C]

Crystallization

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Crystallization on EC 3.1.4.54 - N-acetylphosphatidylethanolamine-hydrolysing phospholipase D

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

Q6IQ20

752275