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Literature summary for 3.1.1.47 extracted from

  • Pande, A.H.; Tillu, V.A.
    Membrane lipid composition differentially modulates the function of human plasma platelet activating factor-acetylhydrolase (2011), Biochim. Biophys. Acta, 1811, 46-56.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information membrane binding of HpPAF-AH increases the activity of enzyme, by interfacial activation. The lipid composition of membrane vesicles, by changing the physicochemical properties, differentially modulates the binding, partial membrane penetration and the activity of the enzyme, detailed overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Homo sapiens
-
-
membrane membrane binding of HpPAF-AH increases the activity of enzyme, by interfacial activation. The lipid composition of membrane vesicles, by changing the physicochemical properties, differentially modulates the binding, partial membrane penetration and the activity of the enzyme, detailed overview Homo sapiens 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no requirement for Ca2+ Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from plasma Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
plasma
-
Homo sapiens
-

Synonyms

Synonyms Comment Organism
HpPAF-AH
-
Homo sapiens
More the enzyme belongs to group VIIA of the phospholipase A2 superfamily and Homo sapiens
plasma platelet activating factor-acetylhydrolase
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Homo sapiens

General Information

General Information Comment Organism
physiological function HpPAF-AH is a calcium-independent phospholipase that catalyzes the hydrolysis of ester bond at the sn-2 position of phospholipid substrates Homo sapiens