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Information on EC 3.1.1.88 - pyrethroid hydrolase
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3.1.1.88 pyrethroid hydrolaseIUBMB Comments
The enzyme is involved in degradation of pyrethroid pesticides. The enzymes from Sphingobium sp., Klebsiella sp. and Aspergillus niger hydrolyse cis-permethrin at approximately equal rate to trans-permethrin [1-3]. The enzyme from mouse hydrolyses trans-permethrin at a rate about 22-fold higher than cis-permethrin .
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Word Map
- 3.1.1.88
-
pyrethroids
-
insecticide
- pesticides
- esterases
- cypermethrin
-
bioremediation
- phenanthroline
-
rho-chloromercuribenzoate
-
rho-nitrophenyl
- ag+
- trans-permethrin
-
organophosphate
- sphingobium
- parathion
- diptera
- fenpropathrin
- fenvalerate
-
activity-based
- deltamethrin
- cis-permethrin
-
marker-free
- environmental protection
- cyhalothrin
-
reusable
-
organophosphorus
- agriculture
- degradation
- food industry
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
pyrethroid hydrolase, pyrethroid-hydrolyzing esterase, permethrinase, sys410, est684, pyrethroid-hydrolyzing carboxylesterase, pyrethroid-hydrolyzing enzyme, esterase sys410, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EstSt7
permethrinase
pyrethroid-hydrolyzing carboxylesterase
pyrethroid-hydrolyzing enzyme
pytH
ST2026
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
trans-permethrin + H2O = (3-phenoxyphenyl)methanol + (1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
pyrethroid-ester hydrolase
The enzyme is involved in degradation of pyrethroid pesticides. The enzymes from Sphingobium sp., Klebsiella sp. and Aspergillus niger hydrolyse cis-permethrin at approximately equal rate to trans-permethrin [1-3]. The enzyme from mouse hydrolyses trans-permethrin at a rate about 22-fold higher than cis-permethrin [4].
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CAS REGISTRY NUMBER
COMMENTARY
77114-04-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(alphaR)-fenpropathrin + H2O
3-phenoxybenzaldehyde + 2,2,3,3-tetramethylcyclopropanecarboxylate + cyanide
both stereoisomers of fenpropathrin: (alphaR)- and (alphaS)-fenpropathrin are hydrolyzed at an appropriately equal rate
-
-
?
(alphaR,2R)-fenvalerate + H2O
3-phenoxybenzaldehyde + (2R)-2-(4-chlorophenyl)-3-methylbutanoate + cyanide
the four stereoisomers of fenvalerate: (alphaS,2R)-fenvalerate, (alphaR,2S)-fenvalerate, (alphaS,2S)-fenvalerate and (alphaR,2R)-fenvalerate are hydrolyzed at an appropriately equal rate
-
-
?
(alphaR,2S)-fenvalerate + H2O
3-phenoxybenzaldehyde + (2S)-2-(4-chlorophenyl)-3-methylbutanoate + cyanide
the four stereoisomers of fenvalerate: (alphaS,2R)-fenvalerate, (alphaR,2S)-fenvalerate, (alphaS,2S)-fenvalerate and (alphaR,2R)-fenvalerate are hydrolyzed at an appropriately equal rate
-
-
?
(alphaS)-fenpropathrin + H2O
3-phenoxybenzaldehyde + 2,2,3,3-tetramethylcyclopropanecarboxylate + cyanide
both stereoisomers of fenpropathrin: (alphaR)- and (alphaS)-fenpropathrin are hydrolyzed at an appropriately equal rate
-
-
?
(alphaS,2R)-fenvalerate + H2O
3-phenoxybenzaldehyde + (2R)-2-(4-chlorophenyl)-3-methylbutanoate + cyanide
the four stereoisomers of fenvalerate: (alphaS,2R)-fenvalerate, (alphaR,2S)-fenvalerate, (alphaS,2S)-fenvalerate and (alphaR,2R)-fenvalerate are hydrolyzed at an appropriately equal rate
-
-
?
(alphaS,2S)-fenvalerate + H2O
3-phenoxybenzaldehyde + (2S)-2-(4-chlorophenyl)-3-methylbutanoate + cyanide
the four stereoisomers of fenvalerate: (alphaS,2R)-fenvalerate, (alphaR,2S)-fenvalerate, (alphaS,2S)-fenvalerate and (alphaR,2R)-fenvalerate are hydrolyzed at an appropriately equal rate
-
-
?
(R/S)-alpha-cyano (6-methoxy-2-naphthyl)-methyl(R/S)-trans/cis-3-(2,2-dibromovinyl)-2,2-dimethyl cyclopropane carboxylate + H2O
?
-
deltamethrin-like substrate
-
-
?
(R/S)-alpha-cyano (6-methoxy-2-naphthyl)-methyl(R/S)-trans/cis-3-(2,2-dichlorovinyl)-2,2-dimethyl cyclopropane carboxylate + H2O
?
-
cypermethrin-like substrate
-
-
?
bifenthrin + H2O
(2-methylbiphenyl-3-yl)methanol + 3-[(1Z)-2-chloro-3,3,3-trifluoroprop-1-en-1-yl]-2,2-dimethylcyclopropanecarboxylate
cis-cypermethrin + H2O
3-phenoxybenzaldehyde + (1S,3S)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
cis-permethrin + H2O
(3-phenoxyphenyl)methanol + (1S,3S)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate
-
-
-
?
cyhalothrin + H2O
3-phenoxybenzaldehyde + 3-[(1Z)-2-chloro-3,3,3-trifluoroprop-1-en-1-yl]-2,2-dimethylcyclopropanecarboxylate + cyanide
cypermethrin + H2O
3-phenoxybenzaldehyde + 3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
deltamethrin + H2O
3-phenoxybenzaldehyde + (1R,3R)-3-(2,2-dibromoethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
fenopropathrin + H2O
3-phenoxybenzaldehyde + 2,2,3,3-tetramethylcyclopropanecarboxylate + cyanide
fenpropathrin + H2O
3-phenoxybenzaldehyde + 2,2,3,3-tetramethylcyclopropanecarboxylate + cyanide
fenvalerate + H2O
3-phenoxybenzaldehyde + 2-(4-chlorophenyl)-3-methylbutanoic acid + cyanide
permethrin + H2O
3-phenoxybenzyl alcohol + 3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate
sumicidin + H2O
3-phenoxybenzaldehyde + 2-(4-chlorophenyl)-3-methylbutanoic acid + cyanide
-
-
-
?
trans-cypermethrin + H2O
3-phenoxybenzaldehyde + (1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
trans-permethrin + H2O
(3-phenoxyphenyl)methanol + (1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate
-
-
-
?
trans-permethrin + H2O
(3-phenoxyphenyl)methanol + trans-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
best substrate for wild-type end mutant enzymes A171V and A171V/D256N
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
about 70% of the activity with 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
highest activity towards 4-nitrophenyl butyrate among all tested 4-nitrophenyl esters
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
low activity, wild-type and mutant enzymes A171V and A171V/D256N
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
about 10% of the activity with 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
low activity, wild-type and mutant enzymes A171V and A171V/D256N
-
-
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
about 5% of the activity with 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
about 85% of the activity with 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
low activity, wild-type and mutant enzymes A171V and A171V/D256N
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
about 35% of the activity with 4-nitrophenyl butyrate
-
-
?
bifenthrin + H2O
(2-methylbiphenyl-3-yl)methanol + 3-[(1Z)-2-chloro-3,3,3-trifluoroprop-1-en-1-yl]-2,2-dimethylcyclopropanecarboxylate
-
-
-
?
bifenthrin + H2O
(2-methylbiphenyl-3-yl)methanol + 3-[(1Z)-2-chloro-3,3,3-trifluoroprop-1-en-1-yl]-2,2-dimethylcyclopropanecarboxylate
-
fenpropathrin is the most preferred substrate. Whereas the hydrolysis rates toward fenpropathrin, permethrin and cypermethrin are not significantly different, fenvalerate, deltamethrin and bifenthrin are degraded at a considerable lower rate than fenpropathrin
-
-
?
bifenthrin + H2O
(2-methylbiphenyl-3-yl)methanol + 3-[(1Z)-2-chloro-3,3,3-trifluoroprop-1-en-1-yl]-2,2-dimethylcyclopropanecarboxylate
-
fenpropathrin is the most preferred substrate. Whereas the hydrolysis rates toward fenpropathrin, permethrin and cypermethrin are not significantly different, fenvalerate, deltamethrin and bifenthrin are degraded at a considerable lower rate than fenpropathrin
-
-
?
cyhalothrin + H2O
3-phenoxybenzaldehyde + 3-[(1Z)-2-chloro-3,3,3-trifluoroprop-1-en-1-yl]-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
cyhalothrin + H2O
3-phenoxybenzaldehyde + 3-[(1Z)-2-chloro-3,3,3-trifluoroprop-1-en-1-yl]-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
cyhalothrin + H2O
3-phenoxybenzaldehyde + 3-[(1Z)-2-chloro-3,3,3-trifluoroprop-1-en-1-yl]-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
cypermethrin + H2O
3-phenoxybenzaldehyde + 3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
fenpropathrin is the most preferred substrate. Whereas the hydrolysis rates toward fenpropathrin, permethrin and cypermethrin are not significantly different, fenvalerate, deltamethrin and bifenthrin are degraded at a considerable lower rate than fenpropathrin
-
-
?
cypermethrin + H2O
3-phenoxybenzaldehyde + 3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
fenpropathrin is the most preferred substrate. Whereas the hydrolysis rates toward fenpropathrin, permethrin and cypermethrin are not significantly different, fenvalerate, deltamethrin and bifenthrin are degraded at a considerable lower rate than fenpropathrin
-
-
?
cypermethrin + H2O
3-phenoxybenzaldehyde + 3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
cypermethrin + H2O
3-phenoxybenzaldehyde + 3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
cypermethrin + H2O
3-phenoxybenzaldehyde + 3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
cypermethrin + H2O
3-phenoxybenzaldehyde + 3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
deltamethrin + H2O
3-phenoxybenzaldehyde + (1R,3R)-3-(2,2-dibromoethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
-
?
deltamethrin + H2O
3-phenoxybenzaldehyde + (1R,3R)-3-(2,2-dibromoethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
deltamethrin + H2O
3-phenoxybenzaldehyde + (1R,3R)-3-(2,2-dibromoethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
fenpropathrin is the most preferred substrate. Whereas the hydrolysis rates toward fenpropathrin, permethrin and cypermethrin are not significantly different, fenvalerate, deltamethrin and bifenthrin are degraded at a considerable lower rate than fenpropathrin
-
-
?
deltamethrin + H2O
3-phenoxybenzaldehyde + (1R,3R)-3-(2,2-dibromoethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
fenpropathrin is the most preferred substrate. Whereas the hydrolysis rates toward fenpropathrin, permethrin and cypermethrin are not significantly different, fenvalerate, deltamethrin and bifenthrin are degraded at a considerable lower rate than fenpropathrin
-
-
?
deltamethrin + H2O
3-phenoxybenzaldehyde + (1R,3R)-3-(2,2-dibromoethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
deltamethrin + H2O
3-phenoxybenzaldehyde + (1R,3R)-3-(2,2-dibromoethenyl)-2,2-dimethylcyclopropanecarboxylate + cyanide
-
-
-
?
fenopropathrin + H2O
3-phenoxybenzaldehyde + 2,2,3,3-tetramethylcyclopropanecarboxylate + cyanide
-
-
-
?
fenopropathrin + H2O
3-phenoxybenzaldehyde + 2,2,3,3-tetramethylcyclopropanecarboxylate + cyanide
-
-
-
?
fenpropathrin + H2O
3-phenoxybenzaldehyde + 2,2,3,3-tetramethylcyclopropanecarboxylate + cyanide
-
fenpropathrin is the most preferred substrate. Whereas the hydrolysis rates toward fenpropathrin, permethrin and cypermethrin are not significantly different, fenvalerate, deltamethrin and bifenthrin are degraded at a considerable lower rate than fenpropathrin
cyano-3-phenoxybenzyl alcohol is unstable and is transformed spontaneously to 3-phenoxybenzaldehyde
-
?
fenpropathrin + H2O
3-phenoxybenzaldehyde + 2,2,3,3-tetramethylcyclopropanecarboxylate + cyanide
-
fenpropathrin is the most preferred substrate. Whereas the hydrolysis rates toward fenpropathrin, permethrin and cypermethrin are not significantly different, fenvalerate, deltamethrin and bifenthrin are degraded at a considerable lower rate than fenpropathrin
cyano-3-phenoxybenzyl alcohol is unstable and is transformed spontaneously to 3-phenoxybenzaldehyde
-
?
fenvalerate + H2O
3-phenoxybenzaldehyde + 2-(4-chlorophenyl)-3-methylbutanoic acid + cyanide
-
fenpropathrin is the most preferred substrate. Whereas the hydrolysis rates toward fenpropathrin, permethrin and cypermethrin are not significantly different, fenvalerate, deltamethrin and bifenthrin are degraded at a considerable lower rate than fenpropathrin
-
-
?
fenvalerate + H2O
3-phenoxybenzaldehyde + 2-(4-chlorophenyl)-3-methylbutanoic acid + cyanide
-
fenpropathrin is the most preferred substrate. Whereas the hydrolysis rates toward fenpropathrin, permethrin and cypermethrin are not significantly different, fenvalerate, deltamethrin and bifenthrin are degraded at a considerable lower rate than fenpropathrin
-
-
?
fenvalerate + H2O
3-phenoxybenzaldehyde + 2-(4-chlorophenyl)-3-methylbutanoic acid + cyanide
-
-
-
?
permethrin + H2O
3-phenoxybenzyl alcohol + 3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate
-
fenpropathrin is the most preferred substrate. Whereas the hydrolysis rates toward fenpropathrin, permethrin and cypermethrin are not significantly different, fenvalerate, deltamethrin and bifenthrin are degraded at a considerable lower rate than fenpropathrin
-
-
?
permethrin + H2O
3-phenoxybenzyl alcohol + 3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate
-
-
-
?
permethrin + H2O
3-phenoxybenzyl alcohol + 3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate
-
-
-
?
trans-permethrin + H2O
(3-phenoxyphenyl)methanol + trans-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate
-
-
-
-
?
trans-permethrin + H2O
(3-phenoxyphenyl)methanol + trans-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate
-
-
-
-
?
additional information
?
-
-
synthesis of two alpha-cyanoester substrates as surrogates for beta-cypermethrin and deltamethrin. The pyrethroid hydrolase activity of carboxylesterases from the pyrethroid resistant strain hydrolyzing cypermethrin-like or deltamethrin-like substrates is 9.05fold and 13.53fold more efficiently than those from the pyrethroid susceptible strain, respectively
-
-
?
additional information
?
-
the enzyme is involved in degradation of pyrethroids
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of pyrethroids
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
the enzyme is involved in degradation of pyrethroids
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of pyrethroids
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no cofactors or coenzymes are required for permethrinase activity
-
additional information
-
no cofactors or coenzymes are required for the pyrethroid-hydrolysis activity
-
additional information
no cofactors were required for enzyme activity
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tetraethyldiphosphate
-
complete inhibition at 0.1 mM, the enzyme may be a serine esterase
additional information
10 mM EDTA or 10 mM 1,10-phenanthroline have little effect on the enzyme activity (less than 10% inhibition)
-
additional information
-
10 mM EDTA or 10 mM 1,10-phenanthroline have little effect on the enzyme activity (less than 10% inhibition)
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Malaria
Phylogenomics Reveals that Asaia Symbionts from Insects Underwent Convergent Genome Reduction, Preserving an Insecticide-Degrading Gene.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01161
4-nitrophenyl acetate
mutant enzyme A171V/D256N, pH 6.5, 55°C
0.00601
4-nitrophenyl butyrate
pH 6.5, 18°C, soluble enzyme
0.00792
4-nitrophenyl butyrate
pH 6.5, 18°C, immobilized enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
350.15
4-nitrophenyl acetate
mutant enzyme A171V/D256N, pH 6.5, 55°C
403.47
4-nitrophenyl butyrate
pH 6.5, 18°C, immobilized enzyme
417.15
4-nitrophenyl butyrate
pH 6.5, 18°C, soluble enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
77
cyano(6-methoxynaphthalen-2-yl)methyl 2-(4-chlorophenyl)-3-methylbutanoate
-
pH 8.0, 30°C
40
cyano(6-methoxynaphthalen-2-yl)methyl 3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate
-
pH 8.0, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
5.5 - 8
the relative activity of the immobilized enzyme is more than 75% at the pH range between 5.5 and 8.0, while the soluble enzyme attains activity over 50% at the same pH range
4.5 - 8.5
pH 4.5: about 50% of maximal activity, pH 8.5: about 50% of maximal activity, mutant enzyme A171V/D256N
4.5 - 8.5
pH 4.5: about 65% of maximal activity, pH 8.5: about 60% of maximal activity, wild-type enzyme
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 65
35°C: about 75% of maximal activity, 65°C: about 65% of maximal activity, wild-type enzyme
40 - 80
40°C: about 55% of maximal activity, 80°C: about 60% of maximal activity, mutant enzyme A171V/D256N
5 - 45
5°C: about 60% of maximal activity, 45°C: about 50% of maximal activity, immobilized enzyme
8 - 40
8°C: about 55% of maximal activity, 40°C: about 40% of maximal activity, soluble enzyme
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.85
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene (est684) isolated from the Mao-tofu metagenome
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
overexpression of gene MdalphaE7 in CRR strains leads to resistance versus pyrethroid
Show AA Sequence and Transmembrane Helices (233 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A171V
the mutant displays 2.46fold higher catalytic activity with the substrate 4-nitrophenyl acetate
A171V/D256N
the mutant displays 2.46fold higher catalytic activity with the substrate 4-nitrophenyl acetate. The mutant is able to efficiently degrade all the pyrethroids (cyhalothrin, cypermethrin, sumicidin, deltamethrin) tested within a short time, indicating that the mutant possesses broad substrate specificity. It shows a broad substrate specificity. The optimal temperature is 10°C higher than that of the wild-type enzyme (55°C). The half-life at 40-65°C is 3.3-310 times longer. The mutant enzyme has a half-life of 12 h at 70°C while the wild-type Sys410 is completely inactivated at 70°C
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
8 - 10
80°C, 60 min, the enzyme maintains over 80% of its maximal activity
725749
5.5 - 9
4 h, enzyme retains more than 80% of its activity in this range
707224
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
t1/2: 6 h ( immobilized enzyme), 1.5 h (soluble enzyme)
40
T1/2: 72 h (wild-type enzyme Sys410), 236 h (mutant enzyme A171V/D256N)
45
T1/2: 38 h (wild-type enzyme Sys410), 154 h (mutant enzyme A171V/D256N)
50
55
T1/2: 6 h (wild-type enzyme Sys410), 77 h (mutant enzyme A171V/D256N)
60
65
70
50
T1/2: 10 h (wild-type enzyme Sys410), 133 h (mutant enzyme A171V/D256N)
60
T1/2: 84 min (wild-type enzyme Sys410), 53 h (mutant enzyme A171V/D256N)
65
T1/2: 6 min (wild-type enzyme Sys410), 31 h (mutant enzyme A171V/D256N)
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high reusability, the immobilized Est684 (immobilized on on mesoporous silica) retains nearly 54% of its activity after 28 cycles, indicating excellent operational stability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
functional expression of mpd and pytH in Pseudomonas putida KT2440 under the control of a constitutive BioBrick promoter J23119
gene MdalphaE7, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis
-
gene pytH, expression in Sphingobium sp. strain BA3 using vector pRK600. The engineered strain can degrade fenpropathin to a higher degree than the wild-type strain JZ-2, and can degrade 3-phenoxybenzoic acid. The inhibition of pyrethroid hydrolase by 3-phenoxybenzoic acid is eliminated
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
degradation
environmental protection
food industry
high potential for bioremediation of pyrethroid-contaminated vegetables
agriculture
agricultural soils are often co-contaminated with different types of pesticides. For example, organophosphates and pyrethroids usually are applied together for pest control. So far, microorganisms with both OP- and pyrethroid-degrading activity have not been isolated from natural environments. Alternatively, construction of engineered microbes with broad-spectrum pesticide-degrading activity may be a promising strategy for bioremediation of mixed pesticides-contaminated soil. To construct multifunctional pesticide degrading microorganisms, the co-expression of multiple degrading enzymes in a host strain may be a feasible approach. Both MPH and PytH are coexpressed in a soil bacterium Pseudomonas putida KT2440, resulting in an engineered strain with the capability to simultaneously degrade OPs and pyrethroids. Six pesticides (methyl parathion, fenitrothion, chlorpyrifos, permethrin, fenopropathrin, cypermethrin) can be effectively degraded by the engineered Pseudomonas putida KT2440. Therefore, the engineered Pseudomonas putida KT2440 could potentially be applied for in situ bioremediation of soil co-contaminated with organophosphates and pyrethroids
agriculture
-
agricultural soils are often co-contaminated with different types of pesticides. For example, organophosphates and pyrethroids usually are applied together for pest control. So far, microorganisms with both OP- and pyrethroid-degrading activity have not been isolated from natural environments. Alternatively, construction of engineered microbes with broad-spectrum pesticide-degrading activity may be a promising strategy for bioremediation of mixed pesticides-contaminated soil. To construct multifunctional pesticide degrading microorganisms, the co-expression of multiple degrading enzymes in a host strain may be a feasible approach. Both MPH and PytH are coexpressed in a soil bacterium Pseudomonas putida KT2440, resulting in an engineered strain with the capability to simultaneously degrade OPs and pyrethroids. Six pesticides (methyl parathion, fenitrothion, chlorpyrifos, permethrin, fenopropathrin, cypermethrin) can be effectively degraded by the engineered Pseudomonas putida KT2440. Therefore, the engineered Pseudomonas putida KT2440 could potentially be applied for in situ bioremediation of soil co-contaminated with organophosphates and pyrethroids
-
degradation
the enzyme can efficiently hydrolyze a wide range of synthetic pyrethroids including fenpropathrin, permethrin, cypermethrin, cyhalothrin, deltamethrin and bifenthrin, which makes it a potential candidate for the detoxification of pyrethroids for the purpose of biodegradation
degradation
-
the enzyme can efficiently hydrolyze a wide range of synthetic pyrethroids including fenpropathrin, permethrin, cypermethrin, cyhalothrin, deltamethrin and bifenthrin, which makes it a potential candidate for the detoxification of pyrethroids for the purpose of biodegradation
-
environmental protection
-
the engineered Sphingobium sp. strain BA3 is more useful in bioremidation of pyrethroid insecticides-contaminated environment than the wild-type strain JZ-2, overview
environmental protection
the mutant enzyme A171V/D256N is an ideal candidate for the biodegradation of pyrethroids (widely used as insecticides)
environmental protection
-
the engineered Sphingobium sp. strain BA3 is more useful in bioremidation of pyrethroid insecticides-contaminated environment than the wild-type strain JZ-2, overview
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maloney, S.E.; Maule, A.; Smith, A.R.
Purification and preliminary characterization of permethrinase from a pyrethroid-transforming strain of Bacillus cereus
Appl. Environ. Microbiol.
59
2007-2013
1993
Bacillus cereus, Bacillus cereus SM3
brenda
Wang, B.Z.; Guo, P.; Hang, B.J.; Li, L.; He, J.; Li, S.P.
Cloning of a novel pyrethroid-hydrolyzing carboxylesterase gene from Sphingobium sp. strain JZ-1 and characterization of the gene product
Appl. Environ. Microbiol.
75
5496-5500
2009
Sphingobium sp. (C0LA90), Sphingobium sp.
brenda
Guo, P.; Wang, B.; Hang, B.; Li, L.; Ali, W.; He, J.; Li, S.
Pyrethroid-degrading Sphingobium sp. JZ-2 and the purification and characterization of a novel pyrethroid hydrolase
Int. Biodeter. Biodegrad.
63
1107-1112
2009
Sphingobium sp., Sphingobium sp. JZ-2
-
brenda
Zhang, L.; Shi, J.; Shi, X.; Liang, P.; Gao, J.; Gao, X.
Quantitative and qualitative changes of the carboxylesterase associated with beta-cypermethrin resistance in the housefly, Musca domestica (Diptera: Muscidae)
Comp. Biochem. Physiol. B
156
6-11
2010
Musca domestica
brenda
Duan, X.; Zheng, J.; Zhang, J.; Hang, B.; He, J.; Li, S.
Characteristics of a 3-phenoxybenzoic acid degrading-bacterium and the construction of a engineering bacterium
Huan Jing Ke Xue
32
240-246
2011
Sphingobium sp., Sphingobium sp. JZ-2
brenda
Weia, T.; Fenga, S.; Shenb, Y.; Hea, P.; Maa, G.; Yua, X.; Zhang, F.; Mao, D.
Characterization of a novel thermophilic pyrethroid-hydrolyzing carboxylesterase from Sulfolobus tokodaii into a new family
J. Mol. Catal. B
97
225-232
2013
Sulfurisphaera tokodaii (Q96Z02), Sulfurisphaera tokodaii 7 (Q96Z02)
-
brenda
Zhai, Y.; Li, K.; Song, J.; Shi, Y.; Yan, Y.
Molecular cloning, purification and biochemical characterization of a novel pyrethroid-hydrolyzing carboxylesterase gene from Ochrobactrum anthropi YZ-1
J. Hazard. Mater.
221-222
206-212
2012
Brucella anthropi
brenda
Fan, X.; Liu, X.; Huang, R.; Liu, Y.
Identification and characterization of a novel thermostable pyrethroid-hydrolyzing enzyme isolated through metagenomic approach
Microb. Cell Fact.
11
33
2012
Escherichia coli
brenda
Zuo, Z.; Gong, T.; Che, Y.; Liu, R.; Xu, P.; Jiang, H.; Qiao, C.; Song, C.; Yang, C.
Engineering Pseudomonas putida KT2440 for simultaneous degradation of organophosphates and pyrethroids and its application in bioremediation of soil
Biodegradation
26
223-233
2015
Sphingobium wenxiniae (C0LA90), Sphingobium wenxiniae DSM 21828 (C0LA90)
brenda
Fan, X.; Liang, W.; Li, Y.; Li, H.; Liu, X.
Identification and immobilization of a novel cold-adapted esterase, and its potential for bioremediation of pyrethroid-contaminated vegetables
Microb. Cell Fact.
16
149
2017
uncultured microorganism (A0A290U7B6)
brenda
Liu, X.; Liang, M.; Liu, Y.; Fan, X.
Directed evolution and secretory expression of a pyrethroid-hydrolyzing esterase with enhanced catalytic activity and thermostability
Microb. Cell Fact.
16
81
2017
uncultured bacterium (H9CDG2)
brenda
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