10.1021/acs.biochem.8b00145.s001
Andrew
N. Bigley
Andrew
N.
Bigley
Tamari Narindoshvili
Tamari
Narindoshvili
Dao Feng Xiang
Dao Feng
Xiang
Frank M. Raushel
Frank M.
Raushel
Multiple Reaction Products from the Hydrolysis of
Chiral and Prochiral Organophosphate Substrates by the Phosphotriesterase
from <i>Sphingobium</i> sp. TCM1
American Chemical Society
2018
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
2018-03-07 00:00:00
Journal contribution
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.