3.8.1.8: atrazine chlorohydrolase
This is an abbreviated version!
For detailed information about atrazine chlorohydrolase, go to the full flat file.
Word Map on EC 3.8.1.8
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3.8.1.8
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herbicide
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adp
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dechlorination
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hydroxyatrazine
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arthrobacter
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s-triazine
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amidohydrolase
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nocardioides
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melamine
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atrazine-degrading
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bioremediation
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agriculture
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haematococcus
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ametryn
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cyanuric
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aurescens
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phytoremediation
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analysis
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environmental protection
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biotechnology
- 3.8.1.8
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herbicide
- adp
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dechlorination
- hydroxyatrazine
- arthrobacter
- s-triazine
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amidohydrolase
- nocardioides
- melamine
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atrazine-degrading
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bioremediation
- agriculture
- haematococcus
- ametryn
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cyanuric
- aurescens
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phytoremediation
- analysis
- environmental protection
- biotechnology
Reaction
Synonyms
atrazine chlorohydrolase, atrazine chlorohydrolase 2, atrazine dechlorinase, AtzA, AtzB, dechlorinase, atrazine (9CI), hydroxyatrazine N-ethylaminohydrolase, More, triazine hydrolase, TrZN
ECTree
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Engineering
Engineering on EC 3.8.1.8 - atrazine chlorohydrolase
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A170T
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naturally occuring mutation G508A, the mutation confers higher specificity for simazine, albeit not atrazine, and greater affinity for a metal ion required for activity
A296T
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naturally occuring mutation G886A, the mutation confers higher specificity for simazine, albeit not atrazine, and greater affinity for a metal ion required for activity
M256I/P258T/Y261S
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naturally occuring mutations G768C, C722A and A782C
V92L/A170T/A296T
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naturally occuring mutations G274T, G508A, and G886A
A216A/T217D/T219E/A220A/D250D
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site-directed mutagenesis, AtzA-variant 288. Km 49 microM, kcat 4.3 s-1, kcat/Km 88000 s-1*M-1
A216A/T217S/T219H/A220G/D250Y
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site-directed mutagenesis, AtzA-variant 431. Km 76 microM, kcat 8.0 s-1, kcat/Km 110000 s-1*M-1
A216G/T217D/T219A/A220V/D250W
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site-directed mutagenesis, AtzA-variant 305. Km 95 microM, kcat 6.2 s-1, kcat/Km 65000 s-1*M-1
A216G/T217D/T219G/A220H/D250D
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site-directed mutagenesis, AtzA-variant 734. Km 62 microM, kcat 15.1 s-1, kcat/Km 240000 s-1*M-1
A216G/T217D/T219G/A220H/D250G
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site-directed mutagenesis, AtzA-variant 430. Km 90 microM, kcat 12.7 s-1, kcat/Km 140000 s-1*M-1
A216H/T217A/T219E/A220S/D250S
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site-directed mutagenesis, AtzA-variant 662. Km 100 microM, kcat 7.4 s-1, kcat/Km 74000 s-1*M-1
A216S/T217A/T219P/A220F/D250G
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site-directed mutagenesis, AtzA-variant 357. Km 67 microM, kcat 2.3 s-1, kcat/Km 34000 s-1*M-1
A216S/T217D/T219G/A220S/D250D
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site-directed mutagenesis, AtzA-variant 841. Km 105 microM, kcat 8.5 s-1, kcat/Km 81000 s-1*M-1
A216S/T217D/T219V/A220H/D250G
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site-directed mutagenesis, AtzA-variant 297. Km 92 microM, kcat 6.8 s-1, kcat/Km 74000 s-1*M-1
A216Y/T217D/T219Y/A220H/D250V
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site-directed mutagenesis, AtzA-variant 422. Km 92 microM, kcat 6.5 s-1, kcat/Km 71000 s-1*M-1
A216A/T217D/T219E/A220A/D250D
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site-directed mutagenesis, AtzA-variant 288. Km 49 microM, kcat 4.3 s-1, kcat/Km 88000 s-1*M-1
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A216G/T217D/T219A/A220V/D250W
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site-directed mutagenesis, AtzA-variant 305. Km 95 microM, kcat 6.2 s-1, kcat/Km 65000 s-1*M-1
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A216S/T217A/T219P/A220F/D250G
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site-directed mutagenesis, AtzA-variant 357. Km 67 microM, kcat 2.3 s-1, kcat/Km 34000 s-1*M-1
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A216Y/T217D/T219Y/A220H/D250V
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site-directed mutagenesis, AtzA-variant 422. Km 92 microM, kcat 6.5 s-1, kcat/Km 71000 s-1*M-1
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D30G/G147D/G162E/A170V/H406P/V466A
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specific acitivity of the mutant enzyme is 3.2fold higher than activity of wild-type enzyme. The kcat/Km-value is 3.0fold higher than the wild-type value
D30G/I393P/L395S/N429S/V466A
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specific acitivity of the mutant enzyme is 3.5fold higher than activity of wild-type enzyme. The kcat/Km-value is 3.2 fold higher than the wild-type value
D30G/Q71G/M315I/R389C/H399Q/N429S/V466A
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specific acitivity of the mutant enzyme is 2.9fold higher than activity of wild-type enzyme. The kcat/Km-value is 2.6fold higher than the wild-type value
D30G/Q71P/R271C/L288Q/M337T/R389C/H399Q/N429S
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specific acitivity of the mutant enzyme is 2.5fold higher than activity of wild-type enzyme. The kcat/Km-value is 2.6fold higher than the wild-type value
D30G/Q91M/T195A/N429S/M99T/R290H
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specific acitivity of the mutant enzyme is 1.2fold higher than activity of wild-type enzyme. The kcat/Km-value is 1.4fold higher than the wild-type value
G55S/I393W/L395R/M315I/E433K
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specific acitivity of the mutant enzyme is 4.0fold higher than activity of wild-type enzyme. The kcat/Km-value is 3.3 fold higher than the wild-type value
Q71P/D128Y/I194V/T195A/M315I/R389C/H399Q/A470T
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specific acitivity of the mutant enzyme is 2.3fold higher than activity of wild-type enzyme. The kcat/Km-value is 2.7fold higher than the wild-type value
Q71R/V58A/R389C/I209M/E317G
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specific acitivity of the mutant enzyme is 2.4fold higher than activity of wild-type enzyme. The kcat/Km-value is 2.9fold higher than the wild-type value
Q7R/V12A/S307P/M337T/I393R/L395R/S438G/R462W
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specific acitivity of the mutant enzyme is 3.5fold higher than activity of wild-type enzyme. The kcat/Km-value is 3.3fold higher than the wild-type value
V12A/Q71A/M315I/M341V
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specific acitivity of the mutant enzyme is 5.2fold higher than activity of wild-type enzyme. The kcat/Km-value is 3.9fold higher than the wild-type value
V12A/Q71T/A173V/M315I/H399Q/N429S/V466A
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specific acitivity of the mutant enzyme is 2.5fold higher than activity of wild-type enzyme. The kcat/Km-value is 2.7fold higher than the wild-type value
V12A/Q71T/M315I/H399Q/N429S/V466A
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specific acitivity of the mutant enzyme is 2.4fold higher than activity of wild-type enzyme. The kcat/Km-value is 2.6fold higher than the wild-type value
V12A/Q71T/T121A/A173V/M315I/H399Q/N429S/V466A
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specific acitivity of the mutant enzyme is 2.9fold higher than activity of wild-type enzyme. The kcat/Km-value is 3.0fold higher than the wild-type value
V12C/A139P/M315I/R389C/I393E/L395R/F439L
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specific acitivity of the mutant enzyme is 2.2fold higher than activity of wild-type enzyme. The kcat/Km-value is 2.6fold higher than the wild-type value
V12F/D30G/V58A/T121A/I393S/L395H
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specific acitivity of the mutant enzyme is fold 2.4higher than activity of wild-type enzyme. The kcat/Km-value is 2.7fold higher than the wild-type value
V12P/D30G/Q71R/H249Y/270V/R389C/I393P/L395P
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specific acitivity of the mutant enzyme is 4.2fold higher than activity of wild-type enzyme. The kcat/Km-value is 3.4fold higher than the wild-type value
V12T/I393G/R389C/L395W/N429S/L446S/V466A
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specific acitivity of the mutant enzyme is 3.4fold higher than activity of wild-type enzyme. The kcat/Km-value is 3.8fold higher than the wild-type value
E241Q
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site-directed mutagenesis, isosteric substitution of the active site glutamate, the mutant shows a large diminution in activity with ametryn, no detectable activity with atratone, and a 10fold decrease with atrazine compared to the wild-type TrzN. Activity of the mutant is nearly constant from pH 6.0 to pH 10.0, consistent with the loss of a proton donating group
R325S
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site-directed mutagenesis, the mutation results in a 12fold decrease in kcat/Km, largely due to kcat
T325D
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site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
T325E
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site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
E241Q
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site-directed mutagenesis, isosteric substitution of the active site glutamate, the mutant shows a large diminution in activity with ametryn, no detectable activity with atratone, and a 10fold decrease with atrazine compared to the wild-type TrzN. Activity of the mutant is nearly constant from pH 6.0 to pH 10.0, consistent with the loss of a proton donating group
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R325S
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site-directed mutagenesis, the mutation results in a 12fold decrease in kcat/Km, largely due to kcat
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T325D
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site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
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T325E
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site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
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D30G
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
D30G/M315I/R389C/H399Q/N429S/V466A
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
D30G/Q71R/M315I/R389C/H399Q/N429S/V466A
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
F439L
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
H399Q
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
L395P
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
M226V
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
M226V/V278A
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
M315I
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
M315I/H399Q/N429S/V466A
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
M337T
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
N429S
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
Q71R
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
R389S
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
T195A
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
T195A/M337T/F439L
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
V12A
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
V278A
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
V466A
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
V58A/H80R/T121A
random mutagenesis, the enzyme shows altered kinetics and increased activity compared to the wild-type enzyme
additional information
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ongoing maintenance of the original atzA-containing isolate in laboratory culture for 12 years in a medium containing high concentrations of atrazine has led to the fixation of another amino acid substitution that substantially reduces activity for the triazines, effect of the amino acid differences between AtzAWT and AtzACh3 on atrazine and simazine specificities: AtzACh2 and AtzACh3 possess a lowerKd for Fe2+ than the other variants, suggesting that the A296T substitution that differentiates AtzACh2 and AtzACh3 from AtzAWT and AtzACh1 may be responsible for improving the affinity of the enzyme for its metal cofactor
additional information
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A216Y/T217D/T219T/A220H/D250E, site-directed mutagenesis, AtzA best variant consensus
additional information
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A216Y/T217D/T219T/A220H/D250E, site-directed mutagenesis, AtzA best variant consensus
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