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(-)-cocaine + H2O
benzoic acid + methyl (1R,2R,3S,5S)-3-hydroxy-8-methyl-8-azabicyclo[3.2.1]-octane-2-carboxylate
-
-
i.e. ecgonine methyl ester
-
?
(-)-cocaine + H2O
benzoic acid + methyl-(1R,2R,3S,5S)-3-hydroxy-8-methyl-8-azabicyclo[3.2.1]-octane-2-carboxylate
-
-
i.e. ecgonine methyl ester
-
?
(-)-cocaine + H2O
ecgonine methyl ester + benzoate
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
hCE-2 has higher catalytic efficiency for hydrolysis than hCE-1
-
-
?
6-monoacetylmorphine + H2O
morphine + acetate
cocaethylene + H2O
?
cocaethylene is a more potent cocaine metabolite, observed in patients who concurrently abuse cocaine and alcohol
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
ethyl 2-hydroxybenzoate + H2O
ethanol + 2-hydroxybenzoate
ethyl benzoate + H2O
ethanol + benzoate
heroin + H2O
6-monoacetylmorphine + acetate
additional information
?
-
(-)-cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
?
(-)-cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
?
(-)-cocaine + H2O
ecgonine methyl ester + benzoate
(-)-cocaine is the naturally occurring enantiomer. The entire hydrolysis reaction consists of four reaction steps, including the nucleophilic attack on the carbonyl carbon of benzoyl ester group by the hydroxyl group of Ser117, dissociation of benzoyl ester group, nucleophilic attack on the carbonyl carbon of benzoyl ester group by water, and finally dissociation between the (-)-cocaine benzoyl group and Ser117 of CocE. The third reaction step involving the nucleophilic attack of a water molecule is rate-determining
-
-
?
6-monoacetylmorphine + H2O
morphine + acetate
-
-
-
?
6-monoacetylmorphine + H2O
morphine + acetate
hCE-2 has higher catalytic efficiency for hydrolysis than hCE-1
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
hCE-2 exhibits different drug ester substrate specificity from the human liver carboxylesterase hCE-1, which hydrolyzes the methyl ester of cocaine. hCE-2 may play an important role in the degradation of cocaine and heroin in human tissues
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
hCE-2 exhibits different drug ester substrate specificity from the human liver carboxylesterase hCE-1, which hydrolyzes the methyl ester of cocaine
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
CocE is the most efficient native enzyme for metabolizing the naturally occurring cocaine
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
Rhodococcus sp. MB1 is capable of utilizing cocaine as a sole source of carbon and nitrogen for growth. The organism lives in the rhizosphere soil of the tropane alkaloid-producing plant Erythroxylum coca. The cocaine esterase initiates degradation of cocaine, which is hydrolyzed to ecgonine methyl ester and benzoate. Both of these esterolytic products are further metabolized by Rhodococcus sp. strain MB1. This activity is inducible in Rhodococcus sp. strain MB1, since no cocaine esterase activity is observed in cells grown on 15 mM succinate as a sole source of carbon
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
the bacterial cocaine esterase, cocE, hydrolyzes cocaine faster than any other reported cocaine esterase
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
Rhodococcus sp. MB1 is capable of utilizing cocaine as a sole source of carbon and nitrogen for growth. The organism lives in the rhizosphere soil of the tropane alkaloid-producing plant Erythroxylum coca. The cocaine esterase initiates degradation of cocaine, which is hydrolyzed to ecgonine methyl ester and benzoate. Both of these esterolytic products are further metabolized by Rhodococcus sp. strain MB1. This activity is inducible in Rhodococcus sp. strain MB1, since no cocaine esterase activity is observed in cells grown on 15 mM succinate as a sole source of carbon
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
strain MB11L of Pseudomonas maltophilia is capable of using cocaine as its sole carbon and energy source
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
strain MB11L of Pseudomonas maltophilia is capable of using cocaine as its sole carbon and energy source
-
-
?
ethyl 2-hydroxybenzoate + H2O
ethanol + 2-hydroxybenzoate
-
-
-
-
?
ethyl 2-hydroxybenzoate + H2O
ethanol + 2-hydroxybenzoate
-
-
-
-
?
ethyl benzoate + H2O
ethanol + benzoate
-
-
-
-
?
ethyl benzoate + H2O
ethanol + benzoate
-
-
-
-
?
heroin + H2O
6-monoacetylmorphine + acetate
-
-
-
?
heroin + H2O
6-monoacetylmorphine + acetate
hCE-2 has higher catalytic efficiency for hydrolysis than hCE-1
-
-
?
additional information
?
-
heroin hydrolysis to 6-MAM and morphine is accelerated by cholinesterases, including acetylcholinesterase (AChE, EC 3.1.1.7) and/or butyrylcholinesterase (BChE, EC 3.1.1.8)
-
-
?
additional information
?
-
the enzyme activity for converting 6-monoacetylmorphine to morphine is much lower than that for converting heroin to 6-monoacetylmorphine. Substrate specificities compared to acetylcholinesterase (EC 3.1.1.7) and butyrylcholinesterase (EC 3.1.1.8)
-
-
?
additional information
?
-
the cocaine esterase displays low levels of activity with 20 mM atropine, a structurally related tropane alkaloid
-
-
?
additional information
?
-
-
the cocaine esterase displays low levels of activity with 20 mM atropine, a structurally related tropane alkaloid
-
-
?
additional information
?
-
the cocaine esterase displays low levels of activity with 20 mM atropine, a structurally related tropane alkaloid
-
-
?
additional information
?
-
-
no activity with: atropine, ethyl 3-hydroxybenzoate or ethyl 4-hydroxybenzoate
-
-
?
additional information
?
-
-
no activity with: atropine, ethyl 3-hydroxybenzoate or ethyl 4-hydroxybenzoate
-
-
?
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(-)-cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
?
6-monoacetylmorphine + H2O
morphine + acetate
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
heroin + H2O
6-monoacetylmorphine + acetate
-
-
-
?
additional information
?
-
heroin hydrolysis to 6-MAM and morphine is accelerated by cholinesterases, including acetylcholinesterase (AChE, EC 3.1.1.7) and/or butyrylcholinesterase (BChE, EC 3.1.1.8)
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
hCE-2 exhibits different drug ester substrate specificity from the human liver carboxylesterase hCE-1, which hydrolyzes the methyl ester of cocaine. hCE-2 may play an important role in the degradation of cocaine and heroin in human tissues
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
CocE is the most efficient native enzyme for metabolizing the naturally occurring cocaine
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
Rhodococcus sp. MB1 is capable of utilizing cocaine as a sole source of carbon and nitrogen for growth. The organism lives in the rhizosphere soil of the tropane alkaloid-producing plant Erythroxylum coca. The cocaine esterase initiates degradation of cocaine, which is hydrolyzed to ecgonine methyl ester and benzoate. Both of these esterolytic products are further metabolized by Rhodococcus sp. strain MB1. This activity is inducible in Rhodococcus sp. strain MB1, since no cocaine esterase activity is observed in cells grown on 15 mM succinate as a sole source of carbon
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
Rhodococcus sp. MB1 is capable of utilizing cocaine as a sole source of carbon and nitrogen for growth. The organism lives in the rhizosphere soil of the tropane alkaloid-producing plant Erythroxylum coca. The cocaine esterase initiates degradation of cocaine, which is hydrolyzed to ecgonine methyl ester and benzoate. Both of these esterolytic products are further metabolized by Rhodococcus sp. strain MB1. This activity is inducible in Rhodococcus sp. strain MB1, since no cocaine esterase activity is observed in cells grown on 15 mM succinate as a sole source of carbon
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
strain MB11L of Pseudomonas maltophilia is capable of using cocaine as its sole carbon and energy source
-
-
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
strain MB11L of Pseudomonas maltophilia is capable of using cocaine as its sole carbon and energy source
-
-
?
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0.0011 - 0.0045
(-)-cocaine
0.15
4-yethylumbelliferyl acetate
pH 7.4, 37°C
0.13 - 0.292
6-monoacetylmorphine
0.0016
cocaethylene
pH 7.4, wild-type enzyme
1.75
ethyl 2-hydroxybenzoate
-
pH 7.0, 30°C
1.89
ethyl benzoate
-
pH 7.0, 30°C
0.0011
(-)-cocaine
-
mutant enzyme A199S/F227A/S287G/A328W/E441D, pH not specified in the publication, at 25°C
0.0031
(-)-cocaine
recombinant enzyme, pH 7.4, 37°C
0.0031
(-)-cocaine
-
mutant enzyme A199S/S287G/A328W/Y332G, at 25°C, in 0.1 M potassium phosphate, pH 7.5
0.0031
(-)-cocaine
-
mutant enzyme A199S/S287G/A328W/Y332G, pH not specified in the publication, at 25°C
0.0035
(-)-cocaine
-
mutant enzyme A199S/F227A/S287G/A328W/Y332G/E441D, pH not specified in the publication, at 25°C
0.0045
(-)-cocaine
-
wild type enzyme, pH not specified in the publication, at 25°C
0.0045
(-)-cocaine
-
wild type enzyme, at 25°C, in 0.1 M potassium phosphate, pH 7.5
0.13
6-monoacetylmorphine
pH 7.4, 37°C
0.292
6-monoacetylmorphine
recombinant enzyme, pH 7.4, 37°C
0.00027
cocaine
pH 7.4, mutant enzyme Q55E
0.00064
cocaine
pH 7.4, wild-type enzyme
0.00075
cocaine
pH 7.4, mutant enzyme Q55A
0.0012
cocaine
pH 7.4, mutant enzyme L407A
0.0015
cocaine
mutant enzyme T172R/G173Q/L196C/I301C, at 37°C, pH not specified in the publication
0.0021
cocaine
mutant enzyme T172R/G173Q/G4C/S10C, at 37°C, pH not specified in the publication
0.0029
cocaine
mutant enzyme T172R/G173Q, at 37°C, pH not specified in the publication
0.0036
cocaine
pH 7.4, mutant enzyme W166A
0.0037
cocaine
mutant enzyme G173Q, at pH 7.4 and 37°C
0.0051
cocaine
pH 7.4, mutant enzyme F408A
0.0057
cocaine
wild type enzyme, at pH 7.4 and 37°C
0.0057
cocaine
-
wild type enzyme, pH not specified in the publication, 37°C
0.0072
cocaine
wild type enzyme, without preincubation, at pH 7.4 and 37°C
0.0073
cocaine
wild type enzyme, after 24 h preincubation at 37°C, at pH 7.4 and 37°C
0.0096
cocaine
pH 7.4, mutant enzyme F261A
0.015
cocaine
ph 7.4, 37°C, mutant enzyme G173Q
0.017
cocaine
mutant enzyme T172R, at pH 7.4 and 37°C
0.017
cocaine
mutant enzyme T172R/G13Q, at pH 7.4 and 37°C
0.019
cocaine
-
pegylated mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
0.021
cocaine
pH 7.4, 37°C, wild-type enzyme
0.021
cocaine
-
mutant enzyme G4C/S10C, pH not specified in the publication, 37°C
0.0229
cocaine
mutant enzyme L169K/G173Q, after 24 h preincubation at 37°C, at pH 7.4 and 37°C
0.024
cocaine
ph 7.4, 37°C, mutant enzyme T172R
0.024
cocaine
ph 7.4, 37°C, mutant enzyme T172R/G173Q
0.026
cocaine
-
mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
0.0288
cocaine
wild type enzyme, at pH 7.4 and 37°C
0.0303
cocaine
mutant enzyme L169K/G173Q, without preincubation, at pH 7.4 and 37°C
0.0305
cocaine
mutant enzyme LMWP-S-S-T172R/G173Q, at pH 7.4 and 37°C
0.0306
cocaine
mutant enzyme T172R/G173Q -YGRKKRRQRRR, at pH 7.4 and 37°C
0.0396
cocaine
mutant enzyme YGRKKRRQRRR-T172R/G173Q, at pH 7.4 and 37°C
0.0415
cocaine
mutant enzyme T172R/G173Q -LMWP, at pH 7.4 and 37°C
0.044
cocaine
mutant enzyme L169K, at pH 7.4 and 37°C
0.046
cocaine
pH 7.4, mutant enzyme S117C
0.049
cocaine
mutant enzyme LMWP-T172R/G173Q, at pH 7.4 and 37°C
0.051
cocaine
pH 7.4, mutant enzyme W151A
0.36
cocaine
-
pH 7.0, 30°C
0.39
cocaine
pH 7.4, 37°C
1.33
cocaine
pH 7.5, 30°C
0.245
heroin
recombinant enzyme, pH 7.4, 37°C
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0.002 - 73.83
(-)-cocaine
0.0037
6-monoacetylmorphine
recombinant enzyme, pH 7.4, 37°C
9.4
cocaethylene
pH 7.4, wild-type enzyme
35.8
heroin
recombinant enzyme, pH 7.4, 37°C
0.002
(-)-cocaine
-
wild type enzyme, pH not specified in the publication, at 25°C
0.068
(-)-cocaine
-
wild type enzyme, at 25°C, in 0.1 M potassium phosphate, pH 7.5
28.83
(-)-cocaine
-
mutant enzyme A199S/F227A/S287G/A328W/E441D, pH not specified in the publication, at 25°C
51
(-)-cocaine
recombinant enzyme, pH 7.4, 37°C
51
(-)-cocaine
-
mutant enzyme A199S/S287G/A328W/Y332G, at 25°C, in 0.1 M potassium phosphate, pH 7.5
51
(-)-cocaine
-
mutant enzyme A199S/S287G/A328W/Y332G, pH not specified in the publication, at 25°C
73.83
(-)-cocaine
-
mutant enzyme A199S/F227A/S287G/A328W/Y332G/E441D, pH not specified in the publication, at 25°C
0.046
cocaine
pH 7.4, mutant enzyme S117C
0.057
cocaine
pH 7.4, mutant enzyme F408A
0.067
cocaine
pH 7.4, mutant enzyme L407A
0.1
cocaine
pH 7.4, mutant enzyme W151A
0.27
cocaine
pH 7.4, mutant enzyme F261A
0.27
cocaine
pH 7.4, mutant enzyme W166A
0.55
cocaine
pH 7.4, mutant enzyme Q55E
1.7
cocaine
pH 7.4, mutant enzyme Q55A
7.8
cocaine
pH 7.4, wild-type enzyme
31.45
cocaine
mutant enzyme T172R/G173Q -YGRKKRRQRRR, at pH 7.4 and 37°C
32.62
cocaine
mutant enzyme YGRKKRRQRRR-T172R/G173Q, at pH 7.4 and 37°C
34.42
cocaine
mutant enzyme LMWP-T172R/G173Q, at pH 7.4 and 37°C
35.17
cocaine
mutant enzyme T172R/G173Q -LMWP, at pH 7.4 and 37°C
36.1
cocaine
mutant enzyme G173Q, at pH 7.4 and 37°C
39
cocaine
mutant enzyme T172R/G173Q/G4C/S10C, at 37°C, pH not specified in the publication
39.17
cocaine
mutant enzyme LMWP-S-S-T172R/G173Q, at pH 7.4 and 37°C
40.1
cocaine
-
pegylated mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
43.3
cocaine
mutant enzyme T172R/G173Q, at 37°C, pH not specified in the publication
44.85
cocaine
wild type enzyme, at pH 7.4 and 37°C
49.9
cocaine
-
mutant enzyme G4C/S10C, pH not specified in the publication, 37°C
50.9
cocaine
mutant enzyme T172R, at pH 7.4 and 37°C
51.4
cocaine
wild type enzyme, at pH 7.4 and 37°C
51.4
cocaine
-
wild type enzyme, pH not specified in the publication, 37°C
53.4
cocaine
mutant enzyme T172R/G13Q, at pH 7.4 and 37°C
56.6
cocaine
-
mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
57.7
cocaine
mutant enzyme T172R/G173Q/L196C/I301C, at 37°C, pH not specified in the publication
80.1
cocaine
mutant enzyme L169K, at pH 7.4 and 37°C
2247
cocaine
ph 7.4, 37°C, mutant enzyme T172R/G173Q
2323
cocaine
pH 7.4, 37°C, wild-type enzyme
2384
cocaine
ph 7.4, 37°C, mutant enzyme G173Q
2502
cocaine
ph 7.4, 37°C, mutant enzyme T172R
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15.17 - 30000
(-)-cocaine
0.0005
6-monoacetylmorphine
recombinant enzyme, pH 7.4, 37°C
0.013
heroin
recombinant enzyme, pH 7.4, 37°C
15.17
(-)-cocaine
-
wild type enzyme, at 25°C, in 0.1 M potassium phosphate, pH 7.5
15.17
(-)-cocaine
-
wild type enzyme, pH not specified in the publication, at 25°C
141.7
(-)-cocaine
-
mutant enzyme A328W/Y332A, pH not specified in the publication, at 25°C
233.3
(-)-cocaine
-
mutant enzyme A328W/Y332G, pH not specified in the publication, at 25°C
516.7
(-)-cocaine
-
mutant enzyme F227A/S287G/A328W/Y332M, pH not specified in the publication, at 25°C
16452
(-)-cocaine
recombinant enzyme, pH 7.4, 37°C
16500
(-)-cocaine
-
mutant enzyme A199S/S287G/A328W/Y332G, at 25°C, in 0.1 M potassium phosphate, pH 7.5
16500
(-)-cocaine
-
mutant enzyme A199S/S287G/A328W/Y332G, pH not specified in the publication, at 25°C
16670
(-)-cocaine
-
mutant enzyme A199S/F227L/S287G/A328W/Y332G, pH not specified in the publication, at 25°C
18330
(-)-cocaine
-
mutant enzyme A199S/F227I/S287G/A328W/Y332G, pH not specified in the publication, at 25°C
21670
(-)-cocaine
-
mutant enzyme A199S/F227A/S287G/A328W/Y332G/E441D, pH not specified in the publication, at 25°C
23330
(-)-cocaine
-
mutant enzyme A199S/F227V/S287G/A328W/Y332G, pH not specified in the publication, at 25°C
26670
(-)-cocaine
-
mutant enzyme A199S/F227A/S287G/A328W/E441D, pH not specified in the publication, at 25°C
30000
(-)-cocaine
-
mutant enzyme A199S/F227A/S287G/A328W/Y332G, pH not specified in the publication, at 25°C
702
cocaine
mutant enzyme LMWP-T172R/G173Q, at pH 7.4 and 37°C
823
cocaine
mutant enzyme YGRKKRRQRRR-T172R/G173Q, at pH 7.4 and 37°C
847
cocaine
mutant enzyme T172R/G173Q -LMWP, at pH 7.4 and 37°C
1028
cocaine
mutant enzyme T172R/G173Q -YGRKKRRQRRR, at pH 7.4 and 37°C
1283
cocaine
mutant enzyme LMWP-S-S-T172R/G173Q, at pH 7.4 and 37°C
1560
cocaine
wild type enzyme, at pH 7.4 and 37°C
1840
cocaine
mutant enzyme L169K, at pH 7.4 and 37°C
2110
cocaine
-
pegylated mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
2120
cocaine
-
mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
2380
cocaine
-
mutant enzyme G4C/S10C, pH not specified in the publication, 37°C
3060
cocaine
mutant enzyme T172R, at pH 7.4 and 37°C
3180
cocaine
mutant enzyme T172R/G13Q, at pH 7.4 and 37°C
8990
cocaine
wild type enzyme, at pH 7.4 and 37°C
8990
cocaine
-
wild type enzyme, pH not specified in the publication, 37°C
9880
cocaine
mutant enzyme G173Q, at pH 7.4 and 37°C
15330
cocaine
mutant enzyme T172R/G173Q, at 37°C, pH not specified in the publication
18330
cocaine
mutant enzyme T172R/G173Q/G4C/S10C, at 37°C, pH not specified in the publication
38330
cocaine
mutant enzyme T172R/G173Q/L196C/I301C, at 37°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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A199S/F227A/S287G/A328W/E441D
-
the mutant shows 1730fold improved (-)-cocaine-hydrolyzing activity compared to the wild type enzyme
A199S/F227A/S287G/A328W/Y332G
-
the mutant has a 2020fold improved catalytic efficiency against (-)-cocaine compared to the wild type enzyme
A199S/F227A/S287G/A328W/Y332G/E441D
-
the mutant shows 1390fold improved (-)-cocaine-hydrolyzing activity compared to the wild type enzyme
A199S/F227A/S287G/A328W/Y332G/F329V
-
the mutant has a 121fold improved catalytic efficiency against (-)-cocaine compared to the wild type enzyme
A199S/F227I/S287G/A328W/Y332G
-
the mutant has a 1170fold improved catalytic efficiency against (-)-cocaine compared to the wild type enzyme
A199S/F227L/S287G/A328W/Y332G
-
the mutant has a 1130fold improved catalytic efficiency against (-)-cocaine compared to the wild type enzyme
A199S/F227V/S287G/A328W/Y332G
-
the mutant has a 1490fold improved catalytic efficiency against (-)-cocaine compared to the wild type enzyme
A199S/S287G/A328W/Y332G/L286I
-
the mutant has a 242fold improved catalytic efficiency against (-)-cocaine compared to the wild type enzyme
A328W/Y332A
-
the mutant has a 9.4fold improved catalytic efficiency against (-)-cocaine compared to the wild type enzyme
A328W/Y332G
-
the mutant has a 15fold improved catalytic efficiency against (-)-cocaine compared to the wild type enzyme
F227A/S287G/A328W/Y332M
-
the mutant has a 34fold improved catalytic efficiency against (-)-cocaine compared to the wild type enzyme
D259N
mutation results in more than 1500fold decrease in kcat
F261A
mutant catalyzed the hydrolysis of cocaine with a 29fold lower kcat and 15fold higher KM
F408A
mutant has 8fold increased KM and more than 100fold decrease in kcat
G173Q/L169K
-
the mutant has a half-life of 370 min and 2.9 days at 37°C
G4C/S10C
-
the mutant shows about 4fold reduced catalytic efficiency compared to the wild type enzyme. The mutant retains almost all activity after 7 days of 37°C treatment
H287A
mutation results in more than 1500fold decrease in kcat
L169K
the mutation significantly increases the stability of cocaine esterase over that of wild type enzyme (half-life at 37°C is 570 min). The mutant exhibits about 8fold increase in Km for cocaine compared to the wild type enzyme
L169K/G173Q
highly thermostable mutant with a half-life of 2.9 days at 37°C
L407A
mutant has 2fold increased KM and more than 100fold decrease in kcat
L407A/F408A
attempts to express the L407A/F408A double mutant do not result in any soluble protein
LMWP-S-S-T172R/G173Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
LMWP-T172R/G173Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Q55E
the mutation within the active site of cocE results in a 2fold improvement in KM, but a 14fold loss of kcat
S117A
mutation results in more than 1500fold decrease in kcat, crystal structures of the S117A and Y44F mutants of cocE. The first urea unfolding transition in the S117A mutant is shifted from 0.5 to 1.3 M urea compared to the wild-type, while the second transition, although broader, has a similar transition point
T172R/G173Q -LMWP
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
T172R/G173Q -YGRKKRRQRRR
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
T172R/G173Q /G4C/S10C
the mutant shows improved catalytic efficiency against cocaine by about 20%
T172R/G173Q/L169K
the mutant shows poor enzyme kinetics and does not display enhanced stabilization
T172R/G173Q/L196C/I301C
the mutant has not only considerably extended the in vitro half-life at 37°C to more than 100 days, but also significantly improved catalytic efficiency against cocaine by about 150%
W151A
mutant catalyzed the hydrolysis of cocaine with a 78fold lower kcat and 80fold higher KM
W166A
mutant has a 29fold lower kcat, and a 6fold increased KM
Y44F
mutation results in more than 1500fold decrease in kcat, crystal structures of the S117A and Y44F mutants of cocE. The urea unfolding curve of the Y44F mutant is very similar to the wild-type, and has almost identical transition points
YGRKKRRQRRR-T172R/G173Q
the mutant still maintains 52% of its cocaine-hydrolyzing efficiency even after incubation at 37°C for 24 h
G173Q
-
the mutant does not have any deleterious effects on the catalytic efficiency
-
L169K
-
the mutation significantly increases the stability of cocaine esterase over that of wild type enzyme (half-life at 37°C is 570 min). The mutant exhibits about 8fold increase in Km for cocaine compared to the wild type enzyme
-
L169K/G173Q
-
highly thermostable mutant with a half-life of 2.9 days at 37°C
-
LMWP-S-S-T172R/G173Q
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
LMWP-T172R/G173Q
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
T172R
-
the mutants shows about wild type thermal stability and decreased catalytic efficiency for cocaine
-
T172R/G173Q
-
the mutation extends half-life at 37°C up to 370 min (30fold improvement compared to the wild type stability) and leads to about 3fold decrease of catalytic efficiency for cocaine
-
T172R/G173Q -LMWP
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
T172R/G173Q -YGRKKRRQRRR
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
T172R/G173Q/L169K
-
the mutant shows poor enzyme kinetics and does not display enhanced stabilization
-
YGRKKRRQRRR-T172R/G173Q
-
the mutant still maintains 52% of its cocaine-hydrolyzing efficiency even after incubation at 37°C for 24 h
-
T172R/G173Q
-
the mutant has an improved in vitro half-life of about 6 h at 37°C
-
T172R/G173Q /G4C/S10C
-
the mutant shows improved catalytic efficiency against cocaine by about 20%
-
T172R/G173Q/L196C/I301C
-
the mutant has not only considerably extended the in vitro half-life at 37°C to more than 100 days, but also significantly improved catalytic efficiency against cocaine by about 150%
-
additional information
computational-experimental effort yields a CocE variant with a 30-fold increase in plasma half-life both in vitro and in vivo
A199S/S287G/A328W/Y332G
-
the mutant has a 1080fold improved catalytic efficiency against (-)-cocaine compared to the wild type enzyme
A199S/S287G/A328W/Y332G
-
the mutant shows 1080fold improved (-)-cocaine-hydrolyzing activity compared to the wild type enzyme
A199S/S287G/A328W/Y332G
-
the mutant shows high activity towards (-)-cocaine with about 1080fold (un-fused) and 100fold (when fused with human serum albumin) improved catalytic efficiency compared to the wild type enzyme and also leads to a decrease in catalytic efficiency with acetylthiocholine and butyrylthiocholine
G173Q
kcat and Km-value for cocaine is similar to wild-type value, half-life is increased 7fold compared to wild-type enzyme
G173Q
the mutant does not have any deleterious effects on the catalytic efficiency
T172R
kcat and Km-value for cocaine is similar to wild-type value, half-life is increased 7fold compared to wild-type enzyme
T172R
the mutants shows about wild type thermal stability and decreased catalytic efficiency for cocaine
T172R/G173Q
kcat and Km-value for cocaine is similar to wild-type value, half-life is increased 30fold compared to wild-type enzyme
T172R/G173Q
mutant enzyme with increased half-life
T172R/G173Q
-
the mutant shows about 4fold reduced catalytic efficiency compared to the wild type enzyme. The mutant remains more than 90% active for longer than 40 days at 37°C, representing a more than 4700fold improvement over wild type. PEGylated mutant enzyme retains full in vitro enzymatic activity
T172R/G173Q
the mutation extends half-life at 37°C up to 370 min (30fold improvement compared to the wild type stability) and leads to about 3fold decrease of catalytic efficiency for cocaine
T172R/G173Q
the mutant has an improved in vitro half-life of about 6 h at 37°C
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