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Information on EC 3.1.1.84 - cocaine esterase
for references in articles please use BRENDA:EC3.1.1.84
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.1 Carboxylic-ester hydrolases
3.1.1.84 cocaine esterase
IUBMB Comments
Rhodococcus sp. strain MB1 and Pseudomonas maltophilia strain MB11L can utilize cocaine as sole source of carbon and energy [2,3].
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
- 3.1.1.84
- butyrylcholinesterase
-
addict
-
abuse
-
cocaine-induced
-
overdose
-
cochs
- ecgonine
-
self-administration
-
cocaine-metabolizing
- medicine
- benzoylecgonine
-
helper-dependent
-
anticocaine
-
fc-fused
-
drug-seeking
-
norcocaine
showSynonyms
cocaine esterase, cocaine hydrolase, coch1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cocE
cocE
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cocaine + H2O = ecgonine methyl ester + benzoate
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
cocaine + H2O = ecgonine methyl ester + benzoate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
cocaine benzoylhydrolase
Rhodococcus sp. strain MB1 and Pseudomonas maltophilia strain MB11L can utilize cocaine as sole source of carbon and energy [2,3].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(-)-cocaine + H2O
benzoic acid + methyl (1R,2R,3S,5S)-3-hydroxy-8-methyl-8-azabicyclo[3.2.1]-octane-2-carboxylate
-
Substrates: -
Products: i.e. ecgonine methyl ester
Products: 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
-
Substrates: -
Products: i.e. ecgonine methyl ester
Products: i.e. ecgonine methyl ester
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
Substrates: hCE-2 has higher catalytic efficiency for hydrolysis than hCE-1
Products: -
Products: -
?
cocaethylene + H2O
?
Substrates: cocaethylene is a more potent cocaine metabolite, observed in patients who concurrently abuse cocaine and alcohol
Products: -
Products: -
?
(-)-cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: -
Products: -
Products: -
?
(-)-cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: -
Products: -
Products: -
?
(-)-cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: (-)-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
Products: -
Products: -
?
6-monoacetylmorphine + H2O
morphine + acetate
Substrates: -
Products: -
Products: -
?
6-monoacetylmorphine + H2O
morphine + acetate
Substrates: hCE-2 has higher catalytic efficiency for hydrolysis than hCE-1
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: 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
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: hCE-2 exhibits different drug ester substrate specificity from the human liver carboxylesterase hCE-1, which hydrolyzes the methyl ester of cocaine
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
Substrates: -
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: -
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: -
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: CocE is the most efficient native enzyme for metabolizing the naturally occurring cocaine
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: 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
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: the bacterial cocaine esterase, cocE, hydrolyzes cocaine faster than any other reported cocaine esterase
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: -
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: 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
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Rhodococcus sp. MB1 Bresler
Substrates: -
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
Substrates: -
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
Substrates: strain MB11L of Pseudomonas maltophilia is capable of using cocaine as its sole carbon and energy source
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
Substrates: -
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
Substrates: strain MB11L of Pseudomonas maltophilia is capable of using cocaine as its sole carbon and energy source
Products: -
Products: -
?
ethyl 2-hydroxybenzoate + H2O
ethanol + 2-hydroxybenzoate
-
Substrates: -
Products: -
Products: -
?
ethyl 2-hydroxybenzoate + H2O
ethanol + 2-hydroxybenzoate
-
Substrates: -
Products: -
Products: -
?
ethyl benzoate + H2O
ethanol + benzoate
-
Substrates: -
Products: -
Products: -
?
ethyl benzoate + H2O
ethanol + benzoate
-
Substrates: -
Products: -
Products: -
?
heroin + H2O
6-monoacetylmorphine + acetate
Substrates: hCE-2 has higher catalytic efficiency for hydrolysis than hCE-1
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Substrates: the cocaine esterase displays low levels of activity with 20 mM atropine, a structurally related tropane alkaloid
Products: -
Products: -
?
additional information
?
-
-
Substrates: the cocaine esterase displays low levels of activity with 20 mM atropine, a structurally related tropane alkaloid
Products: -
Products: -
?
additional information
?
-
Substrates: the cocaine esterase displays low levels of activity with 20 mM atropine, a structurally related tropane alkaloid
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with: atropine, ethyl 3-hydroxybenzoate or ethyl 4-hydroxybenzoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with: atropine, ethyl 3-hydroxybenzoate or ethyl 4-hydroxybenzoate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(-)-cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: -
Products: -
Products: -
?
6-monoacetylmorphine + H2O
morphine + acetate
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: 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
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: -
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: CocE is the most efficient native enzyme for metabolizing the naturally occurring cocaine
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: 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
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: -
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Substrates: 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
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
Rhodococcus sp. MB1 Bresler
Substrates: -
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
Substrates: strain MB11L of Pseudomonas maltophilia is capable of using cocaine as its sole carbon and energy source
Products: -
Products: -
?
cocaine + H2O
ecgonine methyl ester + benzoate
-
Substrates: strain MB11L of Pseudomonas maltophilia is capable of using cocaine as its sole carbon and energy source
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
potential inhibitory activity of heroin or 6-monoacetylmorphine against CocH1-catalyzed hydrolysis of another substrate like (-)-cocaine
-
additional information
-
no inhibition by 1 mM eserine or 1 mM p-hydroxymercuribenzoate. Cocaine esterase shows product inhibition with neither benzoate nor ecgonine methyl ester
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cardiotoxicity
Cocaine Hydrolase Gene Transfer Demonstrates Cardiac Safety and Efficacy against Cocaine-Induced QT Prolongation in Mice.
Seizures
A Bacterial Cocaine Esterase Protects Against Cocaine-Induced Epileptogenic Activity and Lethality.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
(-)-cocaine
-
mutant enzyme A199S/F227A/S287G/A328W/E441D, pH not specified in the publication, at 25°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
0.0015
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
0.0072
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
0.019
cocaine
-
pegylated mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
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
0.026
cocaine
-
mutant enzyme T172R/G173Q, pH not specified in the publication, 37°C
0.0303
cocaine
mutant enzyme L169K/G173Q, without preincubation, 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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
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
39
cocaine
mutant enzyme T172R/G173Q/G4C/S10C, at 37°C, pH not specified in the publication
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
49.9
cocaine
-
mutant enzyme G4C/S10C, pH not specified in the publication, 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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
1028
cocaine
mutant enzyme T172R/G173Q -YGRKKRRQRRR, 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
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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
inhibition kinetics, kinetic modelling, overview
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8 - 10.5
pH 7.8: about 50% of maximal activity, pH 10.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE