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Multiple Reaction Products from the Hydrolysis of Chiral and Prochiral Organophosphate Substrates by the Phosphotriesterase from Sphingobium sp. TCM1
journal contribution
posted on 2018-03-07, 00:00 authored by Andrew
N. Bigley, Tamari Narindoshvili, Dao Feng Xiang, Frank M. RaushelThe
phosphotriesterase from Sphingobium sp. TCM1
(Sb-PTE) is notable for its ability to hydrolyze
organophosphates that are not substrates for other enzymes. In an
attempt to determine the catalytic properties of Sb-PTE for hydrolysis of chiral phosphotriesters, we discovered that
multiple phosphodiester products are formed from a single substrate.
For example, Sb-PTE catalyzes the hydrolysis of the RP-enantiomer of methyl cyclohexyl p-nitrophenyl phosphate with exclusive formation of methyl cyclohexyl
phosphate. However, the enzyme catalyzes hydrolysis of the SP-enantiomer of this substrate to an equal mixture
of methyl cyclohexyl phosphate and cyclohexyl p-nitrophenyl
phosphate products. The ability of this enzyme to catalyze the hydrolysis
of a methyl ester at the same rate as the hydrolysis of a p-nitrophenyl ester contained within the same substrate
is remarkable. The overall scope of the stereoselective properties
of this enzyme is addressed with a library of chiral and prochiral
substrates.
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