Literature summary for 3.1.8.2 extracted from

Wymore, T.; Field, M.J.; Langan, P.; Smith, J.C.; Parks, J.M.
Hydrolysis of DFP and the nerve agent (S)-sarin by DFPase proceeds along two different reaction pathways: Implications for engineering bioscavengers (2014), J. Phys. Chem. B, 118, 4479-4489.

Crystallization (Commentary)

Crystallization (Comment)	Organism
quantum mechanical/molecular mechanical umbrella sampling simulations. The mechanism for hydrolysis of diisopropyl fluorophosphate involves nucleophilic attack by Asp229 on phosphorus to form a pentavalent intermediate. P-F bond dissociation then yields a phosphoacyl enzyme intermediate in the rate-limiting step. A water molecule, coordinated to the catalytic Ca2+, donates a proton to Asp121 and then attacks the tetrahedral phosphoacyl intermediate to liberate the diisopropyl phosphate product. The calculated free energy barrier for hydrolysis of (S)-sarin by the same mechanism is highly unfavorable. Hydrolysis of (S)-sarin proceeds by a mechanism in which Asp229 could activate an intervening water molecule for nucleophilic attack on the substrate	Loligo vulgaris

Crystallization (Comment)

Organism

quantum mechanical/molecular mechanical umbrella sampling simulations. The mechanism for hydrolysis of diisopropyl fluorophosphate involves nucleophilic attack by Asp229 on phosphorus to form a pentavalent intermediate. P-F bond dissociation then yields a phosphoacyl enzyme intermediate in the rate-limiting step. A water molecule, coordinated to the catalytic Ca2+, donates a proton to Asp121 and then attacks the tetrahedral phosphoacyl intermediate to liberate the diisopropyl phosphate product. The calculated free energy barrier for hydrolysis of (S)-sarin by the same mechanism is highly unfavorable. Hydrolysis of (S)-sarin proceeds by a mechanism in which Asp229 could activate an intervening water molecule for nucleophilic attack on the substrate

Loligo vulgaris

Organism

Organism	UniProt	Comment	Textmining
Loligo vulgaris	Q7SIG4	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(S)-sarin + H2O	-	Loligo vulgaris	?	the calculated free energy barrier for hydrolysis of (S)-sarin by the mechanism for diiisopropyl fluorophosphate is highly unfavorable. Hydrolysis of (S)-sarin proceeds by a mechanism in which Asp229 could activate an intervening water molecule for nucleophilic attack on the substrate	?
diisopropyl fluorophosphate + H2O	-	Loligo vulgaris	diisopropyl phosphate + fluoride	The mechanism for hydrolysis of diisopropyl fluorophosphate involves nucleophilic attack by Asp229 on phosphorus to form a pentavalent intermediate. P-F bond dissociation then yields a phosphoacyl enzyme intermediate in the rate-limiting step. A water molecule, coordinated to the catalytic Ca2+, donates a proton to Asp121 and then attacks the tetrahedral phosphoacyl intermediate to liberate the diisopropyl phosphate product	?