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Literature summary for 3.1.8.1 extracted from

  • La Du, B.N.; Adkins, S.; Kuo, C.L.; Lipsig, D.
    Studies on human serum paraoxonase/arylesterase (1993), Chem. Biol. Interact., 87, 25-34.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dilauroyl phosphatidylcholine stimulation Homo sapiens
dioleoyl phosphatidylcholine stimulation Homo sapiens
lecithin stimulation Homo sapiens
lysolecithin stimulation Homo sapiens
phosphatidylcholine purified A or B-type esterases are stimulated Homo sapiens
phosphatidylethanolamine stimulation Homo sapiens
phosphatidylglycerol stimulation Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
6-palmityl-ascorbic acid
-
Homo sapiens
phosphatidylserine
-
Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl B-type esterase has relatively higher paraoxonase activity and is stimulated to a greater degree by 1 M NaCl than the A allozyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood serum in serum, the esterase is tightly bound to the high density lipoproteins, particularly apo A-l Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
paraoxon + H2O the enzyme exists in two genetically determined allozymic forms, and these A and B allozymes possess both paraoxonase and arylesterase activities. B-type esterase has relatively higher paraoxonase activity and is stimulated to a greater degree by 1 M NaCl than the A allozyme Homo sapiens diethylphosphate + 4-nitrophenol
-
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