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Literature summary for 3.1.1.47 extracted from

  • Samanta, U.; Bahnson, B.J.
    Crystal structure of human plasma platelet-activating factor acetylhydrolase: structural implication to lipoprotein binding and catalysis (2008), J. Biol. Chem., 283, 31617-31624.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.47

Cloned(Commentary)

Cloned (Comment) Organism
residues 47-429, expression in Escherichia coli cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
a 1.5 A ligand-free crystal structure and a 2.1 A diethyl phosphoryl complex crystal structure of a 43.3 kDa construct, residues 47-429, of PAF acetylhydrolase are reported Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
paraoxon
-
 Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43400
-
 residues 47-429 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
platelet-activating factor + H2O Homo sapiens
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q13093
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
platelet-activating factor + H2O
-
 Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
lipoprotein-associated PLA2
-
 Homo sapiens
PAF acetylhydrolase
-
 Homo sapiens
PLA2
-
 Homo sapiens
plasma PAF-AH
-
 Homo sapiens
plasma platelet-activating factor acetylhydrolase
-
 Homo sapiens
VIIA phospholipase A2
-
 Homo sapiens