Multiple Reaction Products from the Hydrolysis of
Chiral and Prochiral Organophosphate Substrates by the Phosphotriesterase
from <i>Sphingobium</i> sp. TCM1
Andrew
N. Bigley
Tamari Narindoshvili
Dao Feng Xiang
Frank M. Raushel
10.1021/acs.biochem.8b00145.s001
https://acs.figshare.com/articles/journal_contribution/Multiple_Reaction_Products_from_the_Hydrolysis_of_Chiral_and_Prochiral_Organophosphate_Substrates_by_the_Phosphotriesterase_from_i_Sphingobium_i_sp_TCM1/5975305
The
phosphotriesterase from <i>Sphingobium</i> sp. TCM1
(<i>Sb</i>-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 <i>Sb</i>-PTE for hydrolysis of chiral phosphotriesters, we discovered that
multiple phosphodiester products are formed from a single substrate.
For example, <i>Sb</i>-PTE catalyzes the hydrolysis of the <i>R</i><sub>P</sub>-enantiomer of methyl cyclohexyl <i>p</i>-nitrophenyl phosphate with exclusive formation of methyl cyclohexyl
phosphate. However, the enzyme catalyzes hydrolysis of the <i>S</i><sub>P</sub>-enantiomer of this substrate to an equal mixture
of methyl cyclohexyl phosphate and cyclohexyl <i>p</i>-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 <i>p</i>-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.
2018-03-07 00:00:00
TCM 1
Sb
methyl cyclohexyl p
methyl cyclohexyl phosphate
enzyme catalyzes hydrolysis
enantiomer
ester
Prochiral Organophosphate Substrates
ability
nitrophenyl phosphate products
substrate
Multiple Reaction Products
Sphingobium sp
PTE