Literature summary for 3.1.8.1 extracted from

Fairchild, S.Z.; Peterson, M.W.; Hamza, A.; Zhan, C.G.; Cerasoli, D.M.; Chang, W.E.
Computational characterization of how the VX nerve agent binds human serum paraoxonase 1 (2011), J. Mol. Model., 17, 97-109.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
serum	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
O-ethyl-S-[2-(diisopropylamino)ethyl]methylphosphonothioate + H2O	O-ethyl-S-[2-(diisopropylamino)ethyl]methylphosphonothiate's lone oxygen atom has a strong preference for forming a direct electrostatic interaction with PON1's active site calcium ion. Key residues, which interact with VX are E53, H115, N168, F222, N224, L240, D269, I291, F292, and V346. Residue D183 located in PON1's active site may act as a proton donor or accepter during hydrolysis. PON1's flexible loop region acts as a gatekeeper to the active site residues required for binding VX	Homo sapiens	S-[2-(diisopropylamino)ethyl]-methylphosphonothioic acid + ethanol	-	?

Synonyms

Synonyms	Comment	Organism
paraoxonase-1	-	Homo sapiens
PON1	-	Homo sapiens

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Release 2023.1 (January 2023)