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1 ithout adversely affecting hydrolysis of bis-p-nitrophenyl phosphate.
2 nity and reacts faster with Cdc25B than does p-nitrophenyl phosphate.
3 mbda-Pase, which catalyzes hydrolysis of bis-p-nitrophenyl phosphate.
4 2) required for Ni2+-dependent hydrolysis of p-nitrophenyl phosphate.
5 toring of alkaline phosphatase hydrolysis of p-nitrophenyl phosphate.
6 ctivity on any other sugar phosphates, or on p-nitrophenyl phosphate.
7 coli alkaline phosphatases is 10-60% that of p-nitrophenyl phosphate.
8 ainst both purified phosphorylated Cps2D and p-nitrophenyl phosphate.
9 ase activity against the synthetic substrate p-nitrophenyl phosphate.
10 eavy-atom isotope effects with the substrate p-nitrophenyl phosphate.
11 ge of the RNA model compound 2-hydroxypropyl p-nitrophenyl phosphate.
12 ed with ATPase utilization of ATP but not of p-nitrophenyl phosphate.
13 than a conventional colorimetric assay with p-nitrophenyl phosphate.
14 ed for the cyclization/cleavage of 3'-uridyl p-nitrophenyl phosphate.
15 detectable activity with thymidine-3',5'-di(p-nitrophenyl)-phosphate.
16 d ATP, but was inhibited by MJ33 and diethyl p-nitrophenyl phosphate, a serine protease inhibitor.
17 upon the release of p-nitrophenol (pNP) from p-nitrophenyl phosphate, acid phosphatase activity was d
18 nd does not hydrolyze ATP, pyrophosphate, or p-nitrophenyl phosphate, although it hydrolyzes guanosin
19 ssays revealed catalytic activity toward bis-p-nitrophenyl phosphate, an indicator substrate for phos
21 eriments using the small molecule substrates p-nitrophenyl phosphate and 3-O-methylfluorescein phosph
22 he catalytic properties were determined with p-nitrophenyl phosphate and compared to those of the nat
23 phosphorothioate, and the triesters, diethyl p-nitrophenyl phosphate and diethyl p-nitrophenyl phosph
24 ters measured herein for the diesters, ethyl p-nitrophenyl phosphate and ethyl p-nitrophenyl phosphor
25 the hydrolysis reactions of the monoesters, p-nitrophenyl phosphate and p-nitrophenyl phosphorothioa
26 ysis of the wild type and mutant PTP1B using p-nitrophenyl phosphate and phosphotyrosine-containing p
27 of (18)k(nuc) for hydrolysis of thymidine 5'-p-nitrophenyl phosphate and RNA cleavage by the RNase P
28 s, both enzymes were able to dephosphorylate p-nitrophenyl-phosphate and phosphotyrosine-containing s
29 ic phosphatase activity against nonspecific (p-nitrophenyl phosphate) and specific (CTD-PO(4)) substr
30 bda, the recombinant cores could use casein, p-nitrophenyl phosphate, and a wide variety of peptides
31 line phosphatase catalyzes the hydrolysis of p-nitrophenyl phosphate approximately 70 times faster th
32 Michaelis kinetic parameters, measured using p-nitrophenyl phosphate as a substrate, indicated that a
33 e Mn(2+)-dependent phosphatase activity with p-nitrophenyl phosphate as a substrate, showing that thi
37 assays with a low molecular weight substrate p-nitrophenyl phosphate as well as phosphocasein and apo
39 antially altered catalytic activities toward p-nitrophenyl phosphate at pH 5.0, with both mutants exh
40 found that their in vitro sensitivity to bis-p-nitrophenyl phosphate (BNPP), however, was not shared
41 s the cleavage of the DNA model compound bis(p-nitrophenyl) phosphate (BNPP) in 80% DMSO solution at
42 atalytic activity toward the small substrate p-nitrophenyl phosphate, but is completely inactive towa
43 nt acceleration of the rate of hydrolysis of p-nitrophenyl phosphate by added dipolar solvents such a
44 o measured for the reaction of the monoester p-nitrophenyl phosphate by Ce(IV) bis-Tris propane (1.00
45 The assay is based on the hydrolysis of the p-nitrophenyl phosphate by intracellular acid phosphatas
46 ed by the serine protease inhibitor, diethyl p-nitrophenyl phosphate, by the tetrahedral mimic 1-hexa
48 tein was shown to catalyze the hydrolysis of p-nitrophenyl phosphate, dephosphorylate phosphotyrosyl,
49 hospholipids and phosphatase activity toward p-nitrophenyl phosphate, exhibits a visible absorption b
50 ly catalyzes the cleavage of 2-hydroxypropyl p-nitrophenyl phosphate (HPNP) and a number of diribonuc
53 -rate profiles for the hydrolysis of diethyl p-nitrophenyl phosphate (I) and diethyl p-chlorophenyl p
54 te, 1.0 x 10(-2) M MgCl2, and 2.0 x 10(-4) M p-nitrophenyl phosphate in 1.0 M, pH 9.0 Tris buffer as
55 y is sensitive to the serine reagent diethyl p-nitrophenyl phosphate, indicating that RcOBL1 is a ser
56 example, the kcat/Km for SP-(-)-ethyl phenyl p-nitrophenyl phosphate is 1.8 x 10(8) M-1 s-1 but is on
57 tyrosine phosphatase catalyzed hydrolysis of p-nitrophenyl phosphate is characterized with the system
58 k(cat), as well as a large reduction in the p-nitrophenyl phosphate K(m) were observed for certain c
59 ar kinetics toward the artificial substrates p-nitrophenyl phosphate (k(cat)/K(m) = 15-25 M(-1) s(-1)
60 fission than the reaction of the more labile p-nitrophenyl phosphate (leaving group pK(a) = 7.14).
61 ative theoretical study of the hydrolysis of p-nitrophenyl phosphate, methyl phosphate and p-nitrophe
62 ving group were obtained for the reaction of p-nitrophenyl phosphate monoester coordinated to a dinuc
64 By contrast, the hydrolysis of uncomplexed p-nitrophenyl phosphate occurs by a very loose transitio
65 166 is replaced with an alanine, hydrolyzes p-nitrophenyl phosphate only about 3 times faster than p
67 inhibit recombinant human PTP1B using either p-nitrophenyl phosphate or the tyrosine-phosphorylated i
69 ygen atoms in the AP-catalyzed hydrolysis of p-nitrophenyl phosphate (pNPP) and p-nitrophenylsulfate
73 active mutant substrate complex of LTP1 with p-nitrophenyl phosphate (pNPP) at a resolution of 1.7 A.
78 will hydrolyze small acylphosphates such as p-nitrophenyl phosphate (pNPP) in addition to ATP and ca
80 PP2A showed identical kinetics using either p-nitrophenyl phosphate (pNPP) or 32P-myelin basic prote
83 ave relied on the highly activated substrate p-nitrophenyl phosphate (pNPP), an aryl phosphate with a
86 The calculated kinetic isotope effects for p-nitrophenyl phosphate provide a means to discriminate
87 atio of activity versus IRS-1 to that versus p-nitrophenyl phosphate, PTP1B remained significantly mo
88 The enzyme catalyzes the rapid hydrolysis of p-nitrophenyl phosphate, ribose-5-phosphate, and phospho
89 ered with ATPase utilization of both ATP and p-nitrophenyl phosphate substrates, whereas derivatizati
90 ability to hydrolyze the phosphate group in p-nitrophenyl phosphate suggesting it had a critical rol
91 dition to the general phosphatase substrate, p-nitrophenyl phosphate, the heterodimeric form of the e
92 , binding limits k(cat)/K(m) for reaction of p-nitrophenyl phosphate, the most commonly employed subs
94 We report that CthPnkp also converts bis-p-nitrophenyl phosphate to p-nitrophenol and inorganic p
95 o HePTP on the HePTP-catalyzed hydrolysis of p-nitrophenyl phosphate, Tyr(P) peptides, and its physio
96 yl, ethyl, phenethyl, propargyl, phenyl, and p-nitrophenyl phosphate using [(16)O(18)O] labeled speci
97 as well as weak phosphatase activity toward p-nitrophenyl phosphate (V(max) = 0.08 micro mol/min. mg
98 60A for the S(P)-enantiomer of methyl phenyl p-nitrophenyl phosphate was 13000-fold greater than that
99 sly, the metal complex of the diester methyl-p-nitrophenyl phosphate was found to hydrolyze via a two
101 nhibitor of the PTP1-catalyzed hydrolysis of p-nitrophenyl phosphate with a Ki of 4.9 +/- 0.7 microM.
102 rmined, and the best substrate found was bis(p-nitrophenyl) phosphate with a kcat/Km value of 6.7 x 1
103 ally efficient substrate identified was bis-(p-nitrophenyl) phosphate with a Km of 0.9 mM and a kcat
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