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0.26
-
mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
0.52
-
mutant enzyme D392N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
0.92
-
mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
1.1
-
mutant enzyme R237A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
1.23
-
mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
1.7
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
2.13
-
mutant enzyme H376D, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM MnCl2
2.53
-
mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2
3
6
mutant enzyme H189D, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
3.13
-
mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 8.0),0.5 mM MnCl2
3.33
-
mutant enzyme H189Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
3.63
-
mutant enzyme R237K, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
3.72
-
mutant enzyme H189A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
4.05
-
mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 8.0),0.5 mM MnCl2
8.8
-
mutant enzyme D392E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
9.33
-
mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2
12
-
mutant enzyme H264N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
13.77
-
mutant enzyme D392N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
16.9
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
18
-
mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
19.33
-
mutant enzyme R237A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
23.17
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
33
-
mutant enzyme R237Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
43.5
-
mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
52.33
-
mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
65.83
-
mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
117.5
-
mutant enzyme H189E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
253.3
-
mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
0.033
-
pH 7.3, 22°C, recombinant enzyme
0.8
-
mutant G62V, pH 7.4, 37°C
1.8
-
mutant P178A, pH 7.4, 37°C
2.3
-
mutant F51L, pH 7.4, 37°C
3.1
-
mutant C40G, pH 7.4, 37°C
3.9
-
mutant C25G, pH 7.4, 37°C
4
-
mutant E208A, pH 7.4, 37°C
4.6
-
mutant P64A, pH 7.4, 37°C
7.4
-
wild-type, pH 7.4, 37°C
20.3
-
pH 8.5, 37°C, presence of 0.5 mM phosphate
68.5
-
mutant R252G, pH 7.4, 37°C
105.7
-
+/- 2.8, with 1 mM Ni2+
125.9
-
+/- 8.1, with 20 mM PO43- and 1 mM Ni2+
130.2
-
+/- 8.6, with 50 mM PO43- and 1 mM Ni2+
12.4
-
wild type enzyme, in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2
72
-
in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2
0.176
-
in the presence of 0.1 mM Zn2+
1.4
-
pH 10.0, Co(II)-substituted enzyme
1.4
-
pH 9.0, Co(II)-substituted enzyme
2
-
pH 11.0, Co(II)-substituted enzyme
2.78
-
in the presence of 0.1 mM Fe2+
0.001
-
mutant D164A, pH 7.1, 25°C, presence of Mn2+
0.001
-
mutant D54A, pH 7.1, 25°C, presence of Mn2+
0.001
-
mutant D80A, pH 7.1, 25°C, presence of Mn2+
0.003
-
mutant H78A, pH 7.1, 25°C, presence of Mn2+
0.03
-
pH 7.2, 25°C, presence of Zn2+
0.13
-
mutant H222A, pH 7.1, 25°C, presence of Mn2+
0.25
-
mutant T75A, pH 7.1, 25°C, presence of Mn2+
0.55
-
mutant H200A, pH 7.1, 25°C, presence of Mn2+
0.88
-
mutant D187A, pH 7.1, 25°C, presence of Mn2+
1.07
-
wild-type, pH 7.1, 25°C, presence of Mn2+
1.19
-
pH 7.2, 25°C, presence of Mn2+
4.1
-
pH 7.2, 25°C, presence of Ni2+
0.0064
-
in presence of Mn-Ni-hetero-dinuclear aminopeptidase
0.01
-
in presence of Ni-Ni-homo-dinuclear aminopeptidase
0.01
-
pH 8.0, 30°C, Ni2+-enzyme
0.016
-
in presence of Mn-Cd-hetero-dinuclear aminopeptidase
0.043
-
in presence of Cd-Cd-homo-dinuclear aminopeptidase
0.043
-
pH 8.0, 30°C, Cd2+-enzyme
0.081
-
in presence of Mn-Mn-homo-dinuclear aminopeptidase
0.087
-
in presence of Mn-Co-hetero-dinuclear aminopeptidase
0.1
-
in presence of Mn-Zn-hetero-dinuclear aminopeptidase
0.21
-
pH 8.0, 30°C, Mn2+-enzyme
0.45
-
in presence of Zn-Zn-homo-dinuclear aminopeptidase
0.45
-
pH 8.0, 30°C, Zn2+-enzyme
0.74
-
in presence of Co-Co-homo-dinuclear aminopeptidase
0.74
-
pH 8.0, 30°C, Co2+-enzyme
44000
-
in 0.1 M glycine.NaOH, pH 8.9, at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.2
-
AthTRZ1-P178A, mutant, bis(p-nitrophenyl)phosphate catalysis
1.8
-
AthTRZ1-R252G, mutant, bis(p-nitrophenyl)phosphate catalysis
3.5
-
AthTRZ1-E208A, mutant, bis(p-nitrophenyl)phosphate catalysis
6
-
AthTRZ1-C40G, mutant, bis(p-nitrophenyl)phosphate catalysis
6.5
-
AthTRZ1-F51L, mutant, bis(p-nitrophenyl)phosphate catalysis
8
-
AthTRZ1-G62V, mutant, bis(p-nitrophenyl)phosphate catalysis
8.5
-
AthTRZ1 wild-type, hydrolysis of phosphodiester bonds of bpNPP, KM value for AthTRZ1 two-fold increased relative to that of the tRNase Z of Escherichia coli
13.2
-
AthTRZ1-C25G, mutant, bis(p-nitrophenyl)phosphate catalysis
22.2
-
AthTRZ1-P64A, mutant, bis(p-nitrophenyl)phosphate catalysis
1.6
-
mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2
2.2
-
mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2
3.4
-
mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
3.6
-
mutant enzyme H189D, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
5
-
mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
5
-
mutant enzyme D392E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
5
-
mutant enzyme H376D, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM MnCl2
6.3
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
6.6
-
mutant enzyme H189A, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM MnCl2
7.2
-
mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
7.4
-
mutant enzyme D392N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
9.6
-
mutant enzyme H264N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
11
-
mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
12
-
mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
12
-
mutant enzyme R237K, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
18
-
mutant enzyme R237A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
18
-
mutant enzyme R237Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2
24
-
mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
26
-
mutant enzyme H189Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
38
-
mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
58
-
mutant enzyme H189E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
88
-
wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2
37
-
pH 7.3, 22°C, recombinant enzyme
0.15
-
+/- 0.01, with 1 mM Ni2+
0.66
-
+/- 0.09, with 20 mM PO43- and 1 mM Ni2+
1.01
-
+/- 0.13, with 50 mM PO43- and 1 mM Ni2+
1.2
-
mutant P178A, pH 7.4, 37°C
1.8
-
mutant R252G, pH 7.4, 37°C
3.5
-
mutant E208A, pH 7.4, 37°C
6
-
mutant C40G, pH 7.4, 37°C
6.5
-
mutant F51L, pH 7.4, 37°C
8
-
mutant G62V, pH 7.4, 37°C
8
-
milk fat globule membrane
8.5
-
wild-type, pH 7.4, 37°C
13.2
-
mutant C25G, pH 7.4, 37°C
14.4
-
cytoplasmic membrane of mammary gland
18.3
-
pH 8.5, 37°C, presence of 0.5 mM phosphate
22.2
-
mutant P64A, pH 7.4, 37°C
0.9
-
wild type enzyme, in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2
9.3
-
in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2
0.6
-
pH 8.0, 0.065 mM Ca2+
3.5
-
in the presence of 0.1 mM Zn2+
7
-
in the presence of 0.1 mM Fe2+
0.68
-
pH 7.2, 25°C, presence of Zn2+
2.3
-
pH 7.2, 25°C, presence of Ni2+
2.4
-
mutant D54A, pH 7.1, 25°C, presence of Mn2+
2.9
-
pH 7.2, 25°C, presence of Mn2+
3
-
mutant H222A, pH 7.1, 25°C, presence of Mn2+
3.4
-
mutant D187A, pH 7.1, 25°C, presence of Mn2+
3.5
-
wild-type, pH 7.1, 25°C, presence of Mn2+
3.7
-
mutant D164A, pH 7.1, 25°C, presence of Mn2+
3.7
-
mutant D80A, pH 7.1, 25°C, presence of Mn2+
3.8
-
mutant H78A, pH 7.1, 25°C, presence of Mn2+
18
-
mutant H200A, pH 7.1, 25°C, presence of Mn2+
28
-
mutant T75A, pH 7.1, 25°C, presence of Mn2+
3.8
-
in presence of Mn-Zn-hetero-dinuclear aminopeptidase
3.9
-
in presence of Mn-Co-hetero-dinuclear aminopeptidase
4.5
-
in presence of Zn-Zn-homo-dinuclear aminopeptidase
4.5
-
pH 8.0, 30°C, Zn2+-enzyme
9.5
-
in presence of Co-Co-homo-dinuclear aminopeptidase
9.5
-
pH 8.0, 30°C, Co2+-enzyme
9.7
-
in presence of Cd-Cd-homo-dinuclear aminopeptidase
9.7
-
pH 8.0, 30°C, Cd2+-enzyme
10.6
-
in presence of Ni-Ni-homo-dinuclear aminopeptidase
10.6
-
pH 8.0, 30°C, Ni2+-enzyme
11
-
in presence of Mn-Cd-hetero-dinuclear aminopeptidase
12
-
pH 8.0, 30°C, Mn2+-enzyme
12.3
-
in presence of Mn-Mn-homo-dinuclear aminopeptidase
12.8
-
in presence of Mn-Ni-hetero-dinuclear aminopeptidase
21.88
-
in 0.1 M glycine-NaOH, pH 8.9, at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-
Inhibition of juvenile hormone carboxyesterase of locust hemolymph by organophosphates in vitro
1975
Pratt, G.E.
Insect Biochem.
5
595-607
Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: Origin and biochemical properties
1988
Vanha-Perttula, T.
Clin. Chim. Acta
177
179-196
Isolation and characterization of dipeptidyl peptidase IV from human placenta
1982
Püschel, G.; Mentlein, R.; Heymann, E.
Eur. J. Biochem.
126
359-365
Purification and immunochemical studies of dipeptidyl peptidase IV from bovine kidney
1992
Brownlees, J.; Williams, C.H.; Brennan, G.P.; Halton, D.W.
Biol. Chem. Hoppe-Seyler
373
911-914
Subcellular localization of non-specific carboxylesterases, acylcarnitine hydrolase, monoacylglycerol lipase and palmitoyl-CoA hydrolase in rat liver
1988
Mentlein, R.; Rix-Matzen, H.; Heymann, E.
Biochim. Biophys. Acta
964
319-328
The isolation and properties of chicken kidney serine ethanolamine phosphate phosphodiesterase
1965
Hagerman, D.D.; Rosenberg, H.; Ennor, A.H.; Schiff, P.; Inoue, S.
J. Biol. Chem.
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1108-1112
rac-Glycerol 1:2-cyclic phosphate 2-phosphodiesterase, a new soluble phosphodiesterase of mammalian tissues
1978
Clarke, N.; Dawson, R.M.C.
Biochem. J.
173
579-589
Studies on lysophospholipases. III. The complete purification of two proteins with lysophospholipase activity from beef liver
1974
De Jong, J.G.N.; van den Bosch, H.; Rijken, D.; van Deenen, L.L.M.
Biochim. Biophys. Acta
369
50-63
O-Acetylation and de-O-acetylation of sialic acids. Purification, characterization, and properties of a glycosylated rat liver esterase specific for 9-O-acetylated sialic acids
1989
Higa, H.H.; Manzi, A.; Varki, A.
J. Biol. Chem.
264
19435-19442
Sialate 9-O-acetylesterase from rat liver
1989
Higa, H.H.; Manzi, A.; Diaz, S.; Varki, A.
Methods Enzymol.
179
409-415
Streptozotocin-induced diabetes: significant changes in the kinetic properties of the soluble form of rat bone alkaline phosphatase
1999
Fernandes, S.S.; Furriel, R.P.M.; Petenusci, S.O.; Leone, F.A.
Biochem. Pharmacol.
58
841-849
Purification and characterization of phytase from cotyledons of germinating soybean seeds
1988
Gibson, D.M.; Ullah, A.H.J.
Arch. Biochem. Biophys.
260
503-513
Purification and properties of a novel nucleotide-hydrolysing enzyme (5'-nucleotidase) from Boophilus microplus
1989
Willadsen, P.; Nielsen, J.M.; Riding, G.A.
Biochem. J.
258
79-85
-
Purification, characterization and biological properties of phosphodiesterase from Russel's viper (Vipera russelli) venom
1998
Tin-Win; Aye-Kyaw; Sanda; San-Aye; Win-Aung; Khin-Pa-Pa-Kyaw; Aung-Myat-Kyaw
The Snake
28
83-89
-
Exonuclease (phosphodiesterase) and other nucleolytic enzymes from venom
1966
Laskowski, M.Sr.in
Procedures in Nucleic Acid Research (Cantoni, G. L. ; Davies, D. R. , eds. )
-
154-184
-
Spleen acid exonuclease
1971
Bernardi, A.; Bernardi, G.
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
329-336
Studies on acid hydrolases. IV. Isolation and characterization of spleen exonuclease
1968
Bernardi, A.; Bernardi, G.
Biochim. Biophys. Acta
155
360-370
-
Spleen acid deoxyribonuclease
1971
Bernarde, G.
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
271-287
A novel acid phosphatase excreted by Penicillium funiculosum that hydrolyzes both phosphodiesters and phosphomonoesters with aryl leaving groups
1989
Yoshida, H.; Oikawa, S.; Ikeda, M.; Reese,.T.
J. Biochem.
105
794-798
Purification and characterization of acid phosphatase from cotyledons of germinating soybean seeds
1988
Ullah, A.H.J.; Gibson, D.M.
Arch. Biochem. Biophys.
260
514-520
-
Purification and molecular properties of an acid phosphatase from Asclepias curassavica latex
1986
Giordani, R.; Nari, J.; Noat, G.; Sauve, P.
Plant Sci.
43
207-212
-
Purification and characterization of extracellular acid phosphatase of Tetrahymena pyriformis
1984
Banno, Y.; Nozawa, Y.
Biochim. Biophys. Acta
799
20-28
Purification and properties of one component of acid phosphatase produced by Aspergillus niger
1977
Shimada, Y.; Shinmyo, A.; Enatsu, T.
Biochim. Biophys. Acta
480
417-427
-
Acid phosphatase isoenzymes of Xenopus laevis tadpole tails. Separation and partial characterization
1973
Filburn, C.R.
Arch. Biochem. Biophys.
159
683-693
Acid phosphatase in Schizosaccharomyces pombe. I. Regulation and preliminary characterization
1972
Dibenedetto, G.
Biochim. Biophys. Acta
286
363-374
A nuclease specific for heat denaturated DNA isolated from a product of Aspergillus oryzae
1966
Ando, T.
Biochim. Biophys. Acta
114
158-168
Partial purification and properties of acid sphingomyelinase from rat liver
1983
Watanabe, K.; Sakuragawa, N.; Arima, M.; Satoyoshi, E.
J. Lipid Res.
24
596-603
Acid sphingomyelinase of human placenta: purification, properties, and 125iodine labeling
1982
Sakuragawa, N.
J. Biochem.
92
637-646
Purification of sphingomyelinase to apparent homogeneity by using hydrophobic chromatography
1981
Jones, C.S.; Shankaran, P.; Callahan, J.W.
Biochem. J.
195
373-382
-
Nucleoside cyclic phosphate diesterases
1971
Drummond, G.I.; Yamamoto, M.
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
355-371
A new cyclic phosphodiesterase having a 3'-nucleotidase activity from Escherichia coli B. II. FURTHER STUDIES ON SUBSTRATE SPECIFICITY AND MODE OF ACTION OF THE ENZYME
1964
Anraku, Y.
J. Biol. Chem.
239
3420-3424
A cyclic phosphodiesterase with 3-nucleotidase activity from Proteus mirabilis
1968
Center, M.S.; Behal, F.J.
J. Biol. Chem.
243
138-143
Chloride ion as a modifier of 2,3-cyclic phosphodiesterase purified from halophilic Vibrio alginolyticus
1969
Unemoto, T.; Hayashi, M.
Biochim. Biophys. Acta
171
89-102
Studies of the 2:3-cyclic nucleotide phosphodiesterase of Haemophilus influenzae
1985
Anderson, B.M.; Kahn, D.W.; Anderson, C.D.
J. Gen. Microbiol.
131
2041-2045
Purification and properties of cyclic phosphodiesterase: 3-nucleotidase, a periplasmic enzyme of Haemophilus influenzae
1972
Rodden, J.L.; Scocca, J.J.
Arch. Biochem. Biophys.
153
837-844
A new cyclic phosphodiesterase having a 3'-nucleotidase activity from Escherichia coli B. I. PURIFICATION AND SOME PROPERTIES OF THE ENZYME.
1964
Anraku, Y.
J. Biol. Chem.
239
3412-3419
Properties of two phosphatases and a cyclic phosphodiesterase of Salmonella typhimurium
1977
Weppelman, R.; Kier, L.D.; Ames, B.N.
J. Bacteriol.
130
411-419
-
Manganese ion-dependent production of phosphodiesterase by alkalophilic Bacillus No. A-40-2 and its properties
1990
Ikura, Y.; Horikoshi, K.
Agric. Biol. Chem.
54
3205-3209
-
Purification and some properties of 2',3'-cyclic phosphodiesterase from the cell-free extract of Bacillus subtilis var. amyloliquefacus
1981
Seki, T.; Fukuda, S.
J. Gen. Appl. Microbiol.
27
487-498
Expression, characterization, and crystallization of a member of the novel phospholipase D family of phosphodiesterases
1997
Zhao, Y.; Stuckey, J.A.; Lohse, D.L.; Dixon, J.E.
Protein Sci.
6
2655-2658
Purification and characterization of esterases D-1 and D-2 from human erythrocytes
1988
Okada, Y.; Wakabayashi, K.
Arch. Biochem. Biophys.
263
130-136
Plant biochemistry of xenobiotics. Purification and properties of a wheat esterase hydrolyzing the plasticizer chemical, bis(2-ethylhexyl)phthalate
1984
Krell, H.W.; Sandermann, H.
Eur. J. Biochem.
143
57-62
Partial purification and characterization of a microsomal carboxylesterase specific for salicylate esters from guinea-pig liver
1984
White, K.N.; Hope, D.B.
Biochim. Biophys. Acta
785
138-147
Carboxylesterases-amidases
1981
Heymann, E.; Mentlein, R.
Methods Enzymol.
77
333-344
Different forms of pig liver esterase
1980
Farb, D.; Jencks, W.P.
Arch. Biochem. Biophys.
203
214-226
Characterization of the isoenzymes of pig-liver esterase. 2. Kinetic studies
1979
Junge, W.; Heymann, E.
Eur. J. Biochem.
95
519-525
Esterase XXVII. Purification and characterization of esterase-9A of mouse kidney
1978
Goeppinger, A.; Riebschlaeger, M.; Ronai, A.; von Deimling, O.
Biochim. Biophys. Acta
525
74-86
Purification and characterization of pranlukast hydrolase from rat liver microsomes: the hydrolase is identical to carboxylesterase pI 6.2
1997
Luan, L.; Sugiyama, T.; Takai, S; Usami, Y.; Adachi, T.; Katagiri, Y.; Hirano, K.
Biol. Pharm. Bull.
20
71-75
Purification and characterisation of a mosquito carboxylesterase involved in insecticide resistance
1991
Ketterman, A.J.; Jayawardena, K.G.I.; Hemingway, J.
Biochem. Soc. Trans.
19
305S
-
Comparative study of the enzymatic properties of phosphodiesterases I from the plasma membrane of lactating bovine mammary gland and bovine milk fat globule membrane
1989
Kanno, C.; Ohmura, Y.; Yanagisawa, H.
Agric. Biol. Chem.
53
607-613
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Nucleotide pyrophosphatase/phosphodiesterase 1 exerts a negative effect on starch accumulation and growth in rice seedlings under high temperature and CO2 concentration conditions
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Contribution of carboxylesterase and cytochrome P450 to the bioactivation and detoxification of isocarbophos and its enantiomers in human liver microsomes
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Catalytic and substrate promiscuity distinct multiple chemistries catalysed by the phosphatase domain of receptor protein tyrosine phosphatase
2016
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Identification of inhibitors of the dNTP triphosphohydrolase SAMHD1 using a novel and direct high-throughput assay
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Biochemistry
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Design, synthesis, and structure-activity relationship study of glycyrrhetinic acid derivatives as potent and selective inhibitors against human carboxylesterase 2
2016
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Expression and characterization of a novel glycerophosphodiester phosphodiesterase from Pyrococcus furiosus DSM 3638 that possesses lysophospholipase D activity
2016
Wang, F.; Lai, L.; Liu, Y.; Yang, B.; Wang, Y.
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2016
Gorelik, A.; Heinz, L.X.; Illes, K.; Superti-Furga, G.; Nagar, B.
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Crystal structure of the human alkaline sphingomyelinase provides insights into substrate recognition
2017
Gorelik, A.; Liu, F.; Illes, K.; Nagar, B.
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Expression of carboxylesterase isozymes and their role in the behavior of a fexofenadine prodrug in rat skin
2016
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J. Pharm. Sci.
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Identification and characterization of a novel carboxylesterase from Phaseolus vulgaris for detection of organophosphate and carbamates pesticides
2018
Yang, X.; Dai, J.; Zhao, S.; Li, R.; Goulette, T.; Chen, X.; Xiao, H.
J. Sci. Food. Agric.
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Identification of the cAMP phosphodiesterase CpdA as novel key player in cAMP-dependent regulation in Corynebacterium glutamicum
2017
Schulte, J.; Baumgart, M.; Bott, M.
Mol. Microbiol.
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Crystal structure of mammalian acid sphingomyelinase
2016
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Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase
2016
Igetei, J.E.; Liddell, S.; El-Faham, M.; Doenhoff, M.J.
Parasitology
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Predominant contributions of carboxylesterase 1 and 2 in hydrolysis of anordrin in humans
2018
Jiang, J.; Chen, X.; Zhong, D.
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Nucleotide pyrophosphatase/phosphodiesterase 1 (NPP1) and its inhibitors
2017
Lee, S.Y.; Mueller, C.E.
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