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1 lve a promiscuous arylesterase activity in a phosphotriesterase.
2 e SsoPox from Sulfolobus solfataricus into a phosphotriesterase.
3 emical constraints within the active site of phosphotriesterase.
4 lyzed more slowly than its enantiomer by the phosphotriesterase.
5 mechanism-based inhibitors for the bacterial phosphotriesterase.
6 the broad substrate specificity exhibited by phosphotriesterase.
7 encies of naturally evolved, metal-dependent phosphotriesterases.
8 ystem to perform the directed evolution of a phosphotriesterase (a bioremediation catalyst) caged in
9 tly discovered family of proteins related to phosphotriesterase, a hydrolytic, bacterial enzyme with
10 tion or exhibit arylsulfatase, lactonase, or phosphotriesterase activities.
11 263I, a variant with increased lactonase and phosphotriesterase activities.
12 were transplanted from PTE to Dr0930, but no phosphotriesterase activity could be detected in the chi
13 hese results support previous proposals that phosphotriesterase activity evolved from an ancestral pa
14                  SsoPox exhibits promiscuous phosphotriesterase activity for the degradation of organ
15 n arylesterase with 60-400-fold decreases in phosphotriesterase activity) and (iii) improvements are
16 , proficient lactonase with promiscuous, low phosphotriesterase activity.
17 discrimination inherent within the bacterial phosphotriesterase and 15 mutant enzymes.
18 uclear metal center similar to that found in phosphotriesterase and dihydroorotase.
19 talytic properties of two bacterial enzymes, phosphotriesterase and organophosphorus anhdrolase, are
20 re shown to be relatively poor substrates of phosphotriesterase and they did not induce any significa
21 No natural substrate has been identified for phosphotriesterase, and it has been suggested that the e
22 at the catalytic properties of the wild-type phosphotriesterase can be exploited for the kinetic reso
23                                              Phosphotriesterase catalyzes the hydrolysis of organopho
24            The structure, similar to that of phosphotriesterase, consists of a long, elliptical alpha
25 2+)-, and Mn(2+)/Mn(2+)-substituted forms of phosphotriesterase determined and refined to a nominal r
26 sized and the stereochemical specificity for phosphotriesterase determined.
27                          Unlike conventional phosphotriesterases employed for biocatalytic NA detecti
28  belong to the family of proteins from which phosphotriesterase evolved.
29 electivity of a set of chiral substrates for phosphotriesterase, for both wild-type and mutant forms
30         We interrogated the evolution of the phosphotriesterase from Pseudomonas diminuta (PdPTE), wh
31                                          The phosphotriesterase from Pseudomonas diminuta catalyzes t
32                                              Phosphotriesterase from Pseudomonas diminuta catalyzes t
33                                          The phosphotriesterase from Pseudomonas diminuta hydrolyzes
34                                The bacterial phosphotriesterase from Pseudomonas diminuta is a zinc m
35 strates for a seventh target, a Zn-dependent phosphotriesterase from Pseudomonas diminuta.
36 chanism of action of the manganese-dependent phosphotriesterase from Sphingobium sp. strain TCM1 that
37                       We find that wild-type phosphotriesterase function could be restored (>10(4)
38 lected from a library of 3.4 x 10(7) mutated phosphotriesterase genes using a novel strategy based on
39 coccus radiodurans (Dr-OPH) with homology to phosphotriesterase has been shown to exhibit activity ag
40                                              Phosphotriesterase homology protein (PHP) is a member of
41 coli open reading frame of unknown function (phosphotriesterase homology protein or PHP).
42 glyphosate N-acetyltransferase, xylanase and phosphotriesterase, in order to improve their activity,
43                                              Phosphotriesterase, isolated from the soil-dwelling bact
44 ated that it has evolved from members of the phosphotriesterase-like lactonase (PLL) family that show
45                  A new representative of the Phosphotriesterase-Like Lactonases (PLLs) family from th
46    PHP, which has 28% sequence identity with phosphotriesterase, may belong to the family of proteins
47 nd Pseudomonas diminuta parathion hydrolase (phosphotriesterase or PTE), an enzyme that hydrolyzes to
48                                       Unlike phosphotriesterase, PHP does not catalyze the hydrolysis
49                                    Bacterial phosphotriesterase (PTE) catalyzes the hydrolysis of a w
50 cide, paraoxon, in a coupled assay involving phosphotriesterase (PTE) enzyme expressed from a separat
51 search of enhanced variants of the bacterial phosphotriesterase (PTE) for the hydrolysis of organopho
52                                The bacterial phosphotriesterase (PTE) from Pseudomonas diminuta catal
53                                              Phosphotriesterase (PTE) from Pseudomonas diminuta catal
54             The active site of the bacterial phosphotriesterase (PTE) from Pseudomonas diminuta conta
55      The amino acid sequence identity to the phosphotriesterase (PTE) from Pseudomonas diminuta is 30
56                                              Phosphotriesterase (PTE) from Pseudomonas diminuta is a
57                                              Phosphotriesterase (PTE) from Pseudomonas diminuta is a
58 logue (cyclosarin), and kinetic studies with phosphotriesterase (PTE) from Pseudomonas diminuta, and
59                                              Phosphotriesterase (PTE) from soil bacteria is known for
60                                              Phosphotriesterase (PTE) is a binuclear metalloenzyme th
61                                              Phosphotriesterase (PTE) is an enzyme capable of detoxif
62                                   The enzyme phosphotriesterase (PTE) is capable of hydrolyzing VX bu
63                                    Wild-type phosphotriesterase (PTE) preferentially hydrolyzes the R
64 ubstrate reactivity and stereoselectivity of phosphotriesterase (PTE) toward organophosphotriesters c
65 kage and maintain the activity of an enzyme, phosphotriesterase (PTE), under challenging storage cond
66                The kinetic data published on phosphotriesterase (PTE), with various complexed metals,
67 n mechanism of the hydrolysis of paraoxon by phosphotriesterase (PTE).
68           These included putative nucleases, phosphotriesterases, putative phosphonate transporters a
69 ur pruned enzymes exhibited 10(7)-10(8)-fold phosphotriesterase rate enhancements, despite absence of
70 the body mass index associated orphan enzyme phosphotriesterase-related (PTER)(10) is a physiological
71 mology, it has been named mpr56-1 (for mouse phosphotriesterase-related 56-1).
72 eversibility using directed evolution from a phosphotriesterase to an arylesterase, and back, and exa
73 nificantly enhance the ability of the native phosphotriesterase to hydrolyze phosphorus-fluorine bond
74               Increases in the reactivity of phosphotriesterase toward the slower substrates were att
75                   Four mutant enzymes of the phosphotriesterase were constructed in a preliminary att
76               We describe the selection of a phosphotriesterase with a very fast k(cat) (over 10(5) s