Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
386.8
-
A328W/Y332A mutant BChE
0.046
-
pH 7.4, mutant enzyme S117C
0.057
-
pH 7.4, mutant enzyme F408A
0.067
-
pH 7.4, mutant enzyme L407A
0.1
-
pH 7.4, mutant enzyme W151A
0.27
-
pH 7.4, mutant enzyme F261A; pH 7.4, mutant enzyme W166A
0.55
-
pH 7.4, mutant enzyme Q55E
1.7
-
pH 7.4, mutant enzyme Q55A
7.8
-
pH 7.4, wild-type enzyme
31.45
-
mutant enzyme T172R/G173Q -YGRKKRRQRRR, at pH 7.4 and 37°C
32.62
-
mutant enzyme YGRKKRRQRRR-T172R/G173Q, at pH 7.4 and 37°C
34.42
-
mutant enzyme LMWP-T172R/G173Q, at pH 7.4 and 37°C
35.17
-
mutant enzyme T172R/G173Q -LMWP, at pH 7.4 and 37°C
36.1
-
mutant enzyme G173Q, at pH 7.4 and 37°C
39
-
mutant enzyme T172R/G173Q/G4C/S10C, at 37°C, pH not specified in the publication
39.17
-
mutant enzyme LMWP-S-S-T172R/G173Q, at pH 7.4 and 37°C
40.1
-
pegylated mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
43.3
-
mutant enzyme T172R/G173Q, at 37°C, pH not specified in the publication
44.85
-
wild type enzyme, at pH 7.4 and 37°C
49.9
-
mutant enzyme G4C/S10C, pH not specified in the publication, 37°C
50.9
-
mutant enzyme T172R, at pH 7.4 and 37°C
51.4
-
wild type enzyme, pH not specified in the publication, 37°C
51.4
-
wild type enzyme, at pH 7.4 and 37°C
53.4
-
mutant enzyme T172R/G13Q, at pH 7.4 and 37°C
56.6
-
mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
57.7
-
mutant enzyme T172R/G173Q/L196C/I301C, at 37°C, pH not specified in the publication
80.1
-
mutant enzyme L169K, at pH 7.4 and 37°C
2247
-
ph 7.4, 37°C, mutant enzyme T172R/G173Q
2323
-
pH 7.4, 37°C, wild-type enzyme
2384
-
ph 7.4, 37°C, mutant enzyme G173Q
2502
-
ph 7.4, 37°C, mutant enzyme T172R
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.042
-
A328W/Y332A mutant BChE
0.00027
-
pH 7.4, mutant enzyme Q55E
0.00064
-
pH 7.4, wild-type enzyme
0.00075
-
pH 7.4, mutant enzyme Q55A
0.0012
-
pH 7.4, mutant enzyme L407A
0.0015
-
mutant enzyme T172R/G173Q/L196C/I301C, at 37°C, pH not specified in the publication
0.0021
-
mutant enzyme T172R/G173Q/G4C/S10C, at 37°C, pH not specified in the publication
0.0029
-
mutant enzyme T172R/G173Q, at 37°C, pH not specified in the publication
0.0036
-
pH 7.4, mutant enzyme W166A
0.0037
-
mutant enzyme G173Q, at pH 7.4 and 37°C
0.0051
-
pH 7.4, mutant enzyme F408A
0.0057
-
wild type enzyme, pH not specified in the publication, 37°C
0.0057
-
wild type enzyme, at pH 7.4 and 37°C
0.0072
-
wild type enzyme, without preincubation, at pH 7.4 and 37°C
0.0073
-
wild type enzyme, after 24 h preincubation at 37°C, at pH 7.4 and 37°C
0.0096
-
pH 7.4, mutant enzyme F261A
0.015
-
ph 7.4, 37°C, mutant enzyme G173Q
0.017
-
mutant enzyme T172R, at pH 7.4 and 37°C; mutant enzyme T172R/G13Q, at pH 7.4 and 37°C
0.019
-
pegylated mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
0.021
-
pH 7.4, 37°C, wild-type enzyme
0.021
-
mutant enzyme G4C/S10C, pH not specified in the publication, 37°C
0.0229
-
mutant enzyme L169K/G173Q, after 24 h preincubation at 37°C, at pH 7.4 and 37°C
0.024
-
ph 7.4, 37°C, mutant enzyme T172R; ph 7.4, 37°C, mutant enzyme T172R/G173Q
0.026
-
mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
0.0288
-
wild type enzyme, at pH 7.4 and 37°C
0.0303
-
mutant enzyme L169K/G173Q, without preincubation, at pH 7.4 and 37°C
0.0305
-
mutant enzyme LMWP-S-S-T172R/G173Q, at pH 7.4 and 37°C
0.0306
-
mutant enzyme T172R/G173Q -YGRKKRRQRRR, at pH 7.4 and 37°C
0.0396
-
mutant enzyme YGRKKRRQRRR-T172R/G173Q, at pH 7.4 and 37°C
0.0415
-
mutant enzyme T172R/G173Q -LMWP, at pH 7.4 and 37°C
0.044
-
mutant enzyme L169K, at pH 7.4 and 37°C
0.046
-
pH 7.4, mutant enzyme S117C
0.049
-
mutant enzyme LMWP-T172R/G173Q, at pH 7.4 and 37°C
0.051
-
pH 7.4, mutant enzyme W151A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin
1997
Pindel, E.V.; Kedishvili, N.Y.; Abraham, T.L.; Brzezinski, M.R.; Zhang, J.; Dean, R.A.; Bosron, W.F.
J. Biol. Chem.
272
14769-14775
Fatty acid ethyl ester synthase catalyzes the esterification of ethanol to cocaine
1995
Heith, A.M.; Morse, C.R.; Tsujita, T.; Volpacelli, S.A.; Flood, J.G.; Laposata, M.
Biochem. Biophys. Res. Commun.
208
549-554
DNA sequence of butyrylcholinesterase from the rat: expression of the protein and characterization of the properties of rat butyrylcholinesterase
2002
Boeck, A.T.; Schopfer, L.M.; Lockridge, O.
Biochem. Pharmacol.
63
2101-2110
Human carboxylesterase 1: from drug metabolism to drug discovery
2003
Redinbo, M.R.; Bencharit, S.; Potter, P.M.
Biochem. Soc. Trans.
31
620-624
Biochemical characterization and structural analysis of a highly proficient cocaine esterase
2002
Turner, J.M.; Larsen, N.A.; Basran, A.; Barbas, C.F., 3rd; Bruce, N.C.; Wilson, I.A.; Lerner, R.A.
Biochemistry
41
12297-12307
Characterization of equine butyrylcholinesterase disposition in the mouse
2002
Koetzner, L.; Woods, J.H.
Drug Metab. Dispos.
30
724-730
Biochemical characteristics of purified beef liver NADPH-cytochrome P450 reductase
2002
Arinc, E.; Celik, H.
J. Biochem. Mol. Toxicol.
16
286-297
Modeling effects of oxyanion hole on the ester hydrolysis catalyzed by human cholinesterases
2005
Gao, D.; Zhan, C.G.
J. Phys. Chem. B
109
23070-23076
Cocaine induces a mixed lysosomal lipidosis in cultured fibroblasts, by inactivation of acid sphingomyelinase and inhibition of phospholipase A1
2004
Nassogne, M.C.; Lizarraga, C.; N'Kuli, F.; Van Bambeke, F.; Van Binst, R.; Wallemacq, P.; Tulkens, P.M.; Mingeot-Leclercq, M.P.; Levade, T.; Courtoy, P.J.
Toxicol. Appl. Pharmacol.
194
101-110
Increased organophosphate scavenging in a butyrylcholinesterase mutant
2008
Geyer, B.C.; Woods, R.R.; Mor, T.S.
Chem. Biol. Interact.
175
376-379
An albumin-butyrylcholinesterase for cocaine toxicity and addiction: catalytic and pharmacokinetic properties
2008
Gao, Y.; LaFleur, D.; Shah, R.; Zhao, Q.; Singh, M.; Brimijoin, S.
Chem. Biol. Interact.
175
83-87
Thermostable variants of cocaine esterase for long-time protection against cocaine toxicity
2009
Gao, D.; Narasimhan, D.L.; Macdonald, J.; Brim, R.; Ko, M.C.; Landry, D.W.; Woods, J.H.; Sunahara, R.K.; Zhan, C.G.
Mol. Pharmacol.
75
318-323
Structure and catalytic properties of carboxylesterase isozymes involved in metabolic activation of prodrugs
2008
Hosokawa, M.
Molecules
13
412-431
Gene cloning and nucleotide sequencing and properties of a cocaine esterase from Rhodococcus sp. strain MB1
2000
Bresler, M.M.; Rosser, S.J.; Basran, A.; Bruce, N.C.
Appl. Environ. Microbiol.
66
904-908
Purification and characterization of a human liver cocaine carboxylesterase that catalyzes the production of benzoylecgonine and the formation of cocaethylene from alcohol and cocaine
1994
Brzezinski, M.R.; Abraham, T.L.; Stone, C.L.; Dean. R.A.; Bosron, W.F.
Biochem. Pharmacol.
48
1747-1755
Identification of a cocaine esterase in a strain of Pseudomonas maltophilia
1992
Britt, A.J.; Bruce, N.C.; Lowe, C.R.
J. Bacteriol.
174
2087-2094
Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme
2003
Bencharit, S.; Morton, C.L.; Xue, Y.; Potter, P.M.; Redinbo, M.R.
Nat. Struct. Biol.
10
349-356
A thermally stable form of bacterial cocaine esterase: a potential therapeutic agent for treatment of cocaine abuse
2010
Brim, R.L.; Nance, M.R.; Youngstrom, D.W.; Narasimhan, D.; Zhan, C.G.; Tesmer, J.J.; Sunahara, R.K.; Woods, J.H.
Mol. Pharmacol.
77
593-600
Subunit stabilization and pegylation of cocaine esterase improves in vivo residence time
2011
Narasimhan, D.; Collins, G.T.; Nance, M.R.; Nichols, J.; Edwald, E.; Chan, J.; Ko, M.C.; Woods, J.H.; Tesmer, J.J.; Sunahara, R.K.
Mol. Pharmacol.
80
1056-1065
-
Heterologous expression and characterization of the carboxylesterase from Geobacillus stearothermophilus
2010
Sun, J.; Liu, Z.
Prog. Biochem. Biophys.
37
967-974
Structural analysis of thermostabilizing mutations of cocaine esterase
2010
Narasimhan, D.; Nance, M.; Gao, D.; Ko, M.; MacDonald, J.; Tamburi, P.; Yoon, D.; Landry, D.; Woods, J.; Zhan, C.; Tesmer, J.; Sunahara, R.
Protein Eng.
23
537-547
Rational design, preparation, and characterization of a therapeutic enzyme mutant with improved stability and function for cocaine detoxification
2014
Fang, L.; Chow, K.M.; Hou, S.; Xue, L.; Chen, X.; Rodgers, D.W.; Zheng, F.; Zhan, C.G.
ACS Chem. Biol.
9
1764-1772
The fate of bacterial cocaine esterase (CocE): An in vivo study of CocE-mediated cocaine hydrolysis, CocE pharmacokinetics, and CocE elimination
2012
Brim, R.; Noon, K.; Collins, G.; Stein, A.; Nichols, J.; Narasimhan, D.; Ko, M.; Woods, J.; Sunahara, R.
J. Pharmacol. Exp. Ther.
340
83-95
Cell permeable cocaine esterases constructed by chemical conjugation and genetic recombination
2012
Lee, T.Y.; Park, Y.S.; Garcia, G.A.; Sunahara, R.K.; Woods, J.H.; Yang, V.C.
Mol. Pharm.
9
1361-1373
Acute cocaine treatment increases thimet oligopeptidase in the striatum of rat brain
2012
Dalio, F.M.; Visniauskas, B.; Bicocchi, E.S.; Perry, J.C.; Freua, R.; Gesteira, T.F.; Nader, H.B.; Machado, M.F.; Tufik, S.; Ferro, E.S.; Andersen, M.L.; Toledo, C.A.; Chagas, J.R.; Oliveira, V.
Biochem. Biophys. Res. Commun.
419
724-727
The development of bacterial carboxylesterase biological recognition elements for cocaine detection
2018
Mustafa, S.A.
Mol. Biotechnol.
60
601-607
Catalytic reaction mechanism for drug metabolism in human carboxylesterase-1 cocaine hydrolysis pathway
2018
Yao, J.; Chen, X.; Zheng, F.; Zhan, C.G.
Mol. Pharm.
15
3871-3880
HOME
login
history
all enzymes
BRENDA home
close all tables 
open all tables
top
Information
