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1 e SsoPox from Sulfolobus solfataricus into a phosphotriesterase.
2 emical constraints within the active site of phosphotriesterase.
3 lyzed more slowly than its enantiomer by the phosphotriesterase.
4 mechanism-based inhibitors for the bacterial phosphotriesterase.
5 the broad substrate specificity exhibited by phosphotriesterase.
6 ystem to perform the directed evolution of a phosphotriesterase (a bioremediation catalyst) caged in
7 tly discovered family of proteins related to phosphotriesterase, a hydrolytic, bacterial enzyme with
10 were transplanted from PTE to Dr0930, but no phosphotriesterase activity could be detected in the chi
11 hese results support previous proposals that phosphotriesterase activity evolved from an ancestral pa
16 talytic properties of two bacterial enzymes, phosphotriesterase and organophosphorus anhdrolase, are
17 re shown to be relatively poor substrates of phosphotriesterase and they did not induce any significa
18 No natural substrate has been identified for phosphotriesterase, and it has been suggested that the e
19 at the catalytic properties of the wild-type phosphotriesterase can be exploited for the kinetic reso
22 2+)-, and Mn(2+)/Mn(2+)-substituted forms of phosphotriesterase determined and refined to a nominal r
25 electivity of a set of chiral substrates for phosphotriesterase, for both wild-type and mutant forms
32 chanism of action of the manganese-dependent phosphotriesterase from Sphingobium sp. strain TCM1 that
34 lected from a library of 3.4 x 10(7) mutated phosphotriesterase genes using a novel strategy based on
35 coccus radiodurans (Dr-OPH) with homology to phosphotriesterase has been shown to exhibit activity ag
38 glyphosate N-acetyltransferase, xylanase and phosphotriesterase, in order to improve their activity,
40 ated that it has evolved from members of the phosphotriesterase-like lactonase (PLL) family that show
42 PHP, which has 28% sequence identity with phosphotriesterase, may belong to the family of proteins
43 nd Pseudomonas diminuta parathion hydrolase (phosphotriesterase or PTE), an enzyme that hydrolyzes to
46 cide, paraoxon, in a coupled assay involving phosphotriesterase (PTE) enzyme expressed from a separat
47 search of enhanced variants of the bacterial phosphotriesterase (PTE) for the hydrolysis of organopho
54 logue (cyclosarin), and kinetic studies with phosphotriesterase (PTE) from Pseudomonas diminuta, and
60 ubstrate reactivity and stereoselectivity of phosphotriesterase (PTE) toward organophosphotriesters c
61 kage and maintain the activity of an enzyme, phosphotriesterase (PTE), under challenging storage cond
65 ur pruned enzymes exhibited 10(7)-10(8)-fold phosphotriesterase rate enhancements, despite absence of
67 eversibility using directed evolution from a phosphotriesterase to an arylesterase, and back, and exa
68 nificantly enhance the ability of the native phosphotriesterase to hydrolyze phosphorus-fluorine bond
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