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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

Reaction

Atrazine
+
H2O
=
hydroxyatrazine
+
chloride

Synonyms

atrazine chlorohydrolase, atrazine chlorohydrolase 2, atrazine dechlorinase, AtzA, AtzB, dechlorinase, atrazine (9CI), hydroxyatrazine N-ethylaminohydrolase, More, triazine hydrolase, TrZN

ECTree

     3 Hydrolases
         3.8 Acting on halide bonds
             3.8.1 In carbon-halide compounds
                3.8.1.8 atrazine chlorohydrolase

Engineering

Engineering on EC 3.8.1.8 - atrazine chlorohydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A170T
-
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
-
naturally occuring mutation G886A, the mutation confers higher specificity for simazine, albeit not atrazine, and greater affinity for a metal ion required for activity
M155V
-
naturally occuring mutation A463G
M256I/P258T/Y261S
-
naturally occuring mutations G768C, C722A and A782C
P258T
-
naturally occuring mutation C722A
V92L
-
naturally occuring mutation G274T
V92L/A170T/A296T
-
naturally occuring mutations G274T, G508A, and G886A
A216A/T217D/T219E/A220A/D250D
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
site-directed mutagenesis, AtzA-variant 288. Km 49 microM, kcat 4.3 s-1, kcat/Km 88000 s-1*M-1
-
A216G/T217D/T219A/A220V/D250W
-
site-directed mutagenesis, AtzA-variant 305. Km 95 microM, kcat 6.2 s-1, kcat/Km 65000 s-1*M-1
-
A216S/T217A/T219P/A220F/D250G
-
site-directed mutagenesis, AtzA-variant 357. Km 67 microM, kcat 2.3 s-1, kcat/Km 34000 s-1*M-1
-
A216Y/T217D/T219Y/A220H/D250V
-
site-directed mutagenesis, AtzA-variant 422. Km 92 microM, kcat 6.5 s-1, kcat/Km 71000 s-1*M-1
-
D30G/G147D/G162E/A170V/H406P/V466A
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
site-directed mutagenesis, the mutation results in a 12fold decrease in kcat/Km, largely due to kcat
T325D
-
site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
T325E
-
site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
E241Q
-
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
-
site-directed mutagenesis, the mutation results in a 12fold decrease in kcat/Km, largely due to kcat
-
T325D
-
site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
-
T325E
-
site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
-
A170T/M256I/P258T/Y261S
commercially prepared mutant gene
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
A216G/T217D/T219A/A220V/D250W
-
AtzA mutant
A216G/T217D/T219G/A220H/D250D
-
AtzA mutant
A216G/T217D/T219G/A220H/D250G
-
AtzA mutant
A216H/T217A/T219E/A220S/D250S
-
AtzA mutant
A216S/T217A/T219P/A220F/D250G
-
AtzA mutant
A216S/T217D/T219G/A220S
-
AtzA mutant
A216S/T217D/T219V/A220H/D250G
-
AtzA mutant
A216Y/T217D/A220H/D250E
-
AtzA mutant
A216Y/T217D/T219Y/A220H/D250V
-
AtzA mutant
T217D/T219E
-
AtzA mutant
T217S/T219H/A220G/D250Y
-
AtzA mutant
additional information