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2,4-di(N-isobutylamino)-6-hydroxy-1,3,5-triazine + H2O
6-[(2-methylpropyl)amino]-1,3,5-triazine-2,4-diol + isobutylamine
-
-
-
-
?
2,4-di(N-secbutylamino)-6-hydroxy-1,3,5-triazine + H2O
6-[(1-methylpropyl)amino]-1,3,5-triazine-2,4-diol + butan-2-amine
-
-
-
-
?
2,4-di(N-tertbutylamino)-6-hydroxy-1,3,5-triazine + H2O
6-(tert-butylamino)-1,3,5-triazine-2,4-diol + tert-butylamine
-
-
-
-
?
2,4-diamino-6-hydroxy-1,3,5-triazine + H2O
6-amino-1,3,5-triazine-2,4-diol + NH3
-
-
-
-
?
2,4-diethylamino-6-hydroxy-1,3,5-triazine + H2O
6-(methylamino)-1,3,5-triazine-2,4-diol + ethylamine
-
-
-
-
?
2,4-diisopropylamino-6-hydroxy-1,3,5-triazine + H2O
6-[(1-methylethyl)amino]-1,3,5-triazine-2,4-diol + propan-2-amine
-
-
-
-
?
2,4-dimethylamino-6-hydroxy-1,3,5-triazine + H2O
6-(methylamino)-1,3,5-triazine-2,4-diol + methylamine
-
-
-
-
?
2-(N-ethyl-N-methylamino)-4-ethylamino-6-hydroxy-1,3,5-triazine + H2O
6-[ethyl(methyl)amino]-1,3,5-triazine-2,4-diol + ethylamine
-
-
-
-
?
2-(N-ethylamino)-4-hydroxy-6-(N-hydroxyethylamino)-1,3,5-triazine + H2O
6-[(2-hydroxyethyl)amino]-1,3,5-triazine-2,4-diol + ethylamine
-
-
-
-
?
2-(N-ethylamino)-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine + H2O
6-(ethylamino)-1,3,5-triazine-2,4-diol + propan-2-amine
-
-
-
-
?
2-amino-4-chloro-6-hydroxy-1,3,5-triazine + H2O
6-amino-1,3,5-triazine-2,4-diol + Cl-
-
-
-
-
?
2-amino-4-hydroxy-6-(N-hydroxyethylamino)-1,3,5-triazine + H2O
6-[(2-hydroxyethyl)amino]-1,3,5-triazine-2,4-diol + NH3
-
-
-
-
?
2-amino-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine + H2O
6-(isopropylamino)-1,3,5-triazine-2,4-diol + NH3
-
-
-
-
?
2-amino-6-(N-ethylamino)-4-hydroxy-1,3,5-triazine + H2O
6-(ethylamino)-1,3,5-triazine-2,4-diol + NH3
-
-
-
-
?
2-chloro-4-(N-ethylamino)-6-hydroxy-1,3,5-triazine + H2O
6-(ethylamino)-1,3,5-triazine-2,4-diol + Cl-
-
-
-
-
?
2-chloro-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine + H2O
6-(isopropylamino)-1,3,5-triazine-2,4-diol + Cl-
-
-
-
-
?
2-hydroxy-4,6-di(N-hydroxyethylamino)-1,3,5-triazine + H2O
6-[(2-hydroxyethyl)amino]-1,3,5-triazine-2,4-diol + 2-aminoethanol
-
-
-
-
?
2-hydroxy-4-(N-isopropylamino)-6-(N-(3-methoxypropyl)amino)-1,3,5-triazine + H2O
?
-
-
-
-
?
6-(ethylamino)-4-(methylamino)-1,3,5-triazin-2-ol + H2O
6-(ethylamino)-1,3,5-triazine-2,4-diol + methylamine
-
-
-
-
?
6-hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-triazine + H2O
6-[(1-methylethyl)amino]-1,3,5-triazine-2,4-diol + methylamine
-
-
-
-
?
ametryn + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + H-S-CH3
atratone + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + methanol
atrazine + H2O
2-hydroxyatrazine + chloride
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
atrazine + H2O
cyanuric acid + ?
atrazine + H2O
hydroxyatrazine + chloride
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
cyanazine + H2O
2-{[4-(ethylamino)-6-hydroxy-1,3,5-triazin-2-yl]amino}-2-methylpropanenitrile + HCl
desethylatrazine + H2O
2-hydroxy-4-amino-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
hydroxyatrazine + H2O
N-isopropylammelide + ethylamine
-
-
-
-
?
propazine + H2O
4,6-bis(propan-2-ylamino)-1,3,5-triazin-2-ol + HCl
simazine + H2O
4,6-diethylamino-1,3,5-triazine + HCl
terbuthylazine + H2O
?
-
-
-
-
?
atrazine + H2O
additional information
-
ametryn + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + H-S-CH3
-
i.e. 2-thiomethyl-4-isopropylamino-6-ethylamino-1,3,5-triazine, a s-triazine herbicide
-
-
?
ametryn + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + H-S-CH3
-
i.e. 2-thiomethyl-4-isopropylamino-6-ethylamino-1,3,5-triazine, a s-triazine herbicide
-
-
?
atratone + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + methanol
-
-
-
-
?
atratone + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + methanol
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
Clavibacter michiganese
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
Clavibacter michiganese ATZ1
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
-
i.e. 2-chloro-4-isopropylamino-6-ethylamino-1,3,5-triazine, a s-triazine herbicide
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
-
i.e. 2-chloro-4-isopropylamino-6-ethylamino-1,3,5-triazine, a s-triazine herbicide
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
overview, diverse atrazine derivates, i.e. chlorodialkylamino triazines, tested as substrates
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
overview, diverse atrazine derivates, i.e. chlorodialkylamino triazines, tested as substrates
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
overview, diverse atrazine derivates, i.e. chlorodialkylamino triazines, tested as substrates
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
overview, diverse atrazine derivates, i.e. chlorodialkylamino triazines, tested as substrates
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
Clavibacter michiganese
-
utilization of atrazines with Cl exchanged for F, CN, N3, OCH3, SCH3
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
Clavibacter michiganese
-
overview, diverse atrazine derivates, i.e. chlorodialkylamino triazines, tested as substrates
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
Clavibacter michiganese ATZ1
-
utilization of atrazines with Cl exchanged for F, CN, N3, OCH3, SCH3
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
Clavibacter michiganese ATZ1
-
overview, diverse atrazine derivates, i.e. chlorodialkylamino triazines, tested as substrates
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
6-chloro-N2-ethyl-N4-isopropyl-1,3,5-triazine-2,4-diamine, herbicide
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
6-chloro-N2-ethyl-N4-isopropyl-1,3,5-triazine-2,4-diamine, herbicide
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
ir
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
ir
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
overview, diverse atrazine derivates, i.e. chlorodialkylamino triazines, tested as substrates
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
catabolic atrazine degradation pathway, overview, dechlorination
-
-
ir
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
specific for halo-substituted triazine ring compounds, dehalogenation and degradation of the herbicide atrazine
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
specific for halo-substituted triazine ring compounds
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
overview, diverse atrazine derivates, i.e. chlorodialkylamino triazines, tested as substrates
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
overview, diverse atrazine derivates, i.e. chlorodialkylamino triazines, tested as substrates
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
overview, diverse atrazine derivates, i.e. chlorodialkylamino triazines, tested as substrates
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
overview, diverse atrazine derivates, i.e. chlorodialkylamino triazines, tested as substrates
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
cyanuric acid + ?
-
-
-
-
?
atrazine + H2O
cyanuric acid + ?
-
-
-
-
?
atrazine + H2O
hydroxyatrazine + chloride
-
-
-
-
?
atrazine + H2O
hydroxyatrazine + chloride
-
-
-
?
atrazine + H2O
hydroxyatrazine + chloride
the enzyme is involved in mineralization of atrazine
-
-
?
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
-
-
-
-
?
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
-
-
-
-
?
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
-
-
-
-
?
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
-
-
-
-
?
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
-
-
-
-
?
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
-
-
-
-
?
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
-
-
-
-
?
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
-
-
-
-
?
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
-
-
-
-
?
cyanazine + H2O
2-{[4-(ethylamino)-6-hydroxy-1,3,5-triazin-2-yl]amino}-2-methylpropanenitrile + HCl
-
-
-
-
?
cyanazine + H2O
2-{[4-(ethylamino)-6-hydroxy-1,3,5-triazin-2-yl]amino}-2-methylpropanenitrile + HCl
-
-
-
-
?
prometryn + H2O
?
-
-
-
-
?
prometryn + H2O
?
-
-
-
-
?
propazine + H2O
4,6-bis(propan-2-ylamino)-1,3,5-triazin-2-ol + HCl
-
-
-
-
?
propazine + H2O
4,6-bis(propan-2-ylamino)-1,3,5-triazin-2-ol + HCl
-
-
-
-
?
simazine + H2O
4,6-diethylamino-1,3,5-triazine + HCl
-
-
-
-
?
simazine + H2O
4,6-diethylamino-1,3,5-triazine + HCl
-
-
-
-
?
simazine + H2O
4,6-diethylamino-1,3,5-triazine + HCl
-
-
-
-
?
atrazine + H2O
additional information
-
-
-
following metabolites are detected, hydroxyatrazine, desisopropyl atrazine, N-isopropylammelide
-
?
additional information
?
-
-
no activity with melamine and ammeline
-
-
?
additional information
?
-
AtzA can only hydrolyze triazine halides. The relatively high Km of AtzA, which is greater than the water solubility of atrazine, leads to a less efficient catalytic rate by the enzyme compared to the alternative dimeric chlorohydrolase TrzN
-
-
?
additional information
?
-
-
AtzA can only hydrolyze triazine halides. The relatively high Km of AtzA, which is greater than the water solubility of atrazine, leads to a less efficient catalytic rate by the enzyme compared to the alternative dimeric chlorohydrolase TrzN
-
-
?
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0.029
2,4-diisopropylamino-6-hydroxy-1,3,5-triazine
-
deamination
0.02
2-(N-ethylamino)-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine
-
deamination
0.23
2-chloro-4-(N-ethylamino)-6-hydroxy-1,3,5-triazine
-
dechlorination
0.12
2-chloro-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine
-
dechlorination
0.04
6-hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-triazine
-
deamination
additional information
additional information
-
3.9
ametryn
-
wild-type enzyme, pH 7.0, temperature not specified in the publication
7.8
ametryn
-
mutant R325, pH and temperature not specified in the publicationS
0.0238
Atrazine
-
-
0.049
Atrazine
-
A216A/T217D/T219E/A220A/D250D, site-directed mutagenesis, AtzA-variant 288, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.049
Atrazine
-
T217D/T219E, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
0.062
Atrazine
-
A216G/T217D/T219G/A220H/D250D, site-directed mutagenesis, AtzA-variant 734, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.062
Atrazine
-
A216G/T217D/T219G/A220H/D250D, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
0.067
Atrazine
-
A216S/T217A/T219P/A220F/D250G, site-directed mutagenesis, AtzA-variant 357, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.067
Atrazine
-
A216S/T217A/T219P/A220F/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
0.076
Atrazine
-
A216A/T217S/T219H/A220G/D250Y, site-directed mutagenesis, AtzA-variant 431, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.076
Atrazine
-
T217S/T219H/A220G/D250Y, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
0.09
Atrazine
-
A216G/T217D/T219G/A220H/D250G, site-directed mutagenesis, AtzA-variant 430, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.09
Atrazine
-
Q71R/V58A/R389C/I209M/E317G, pH 7.2, 23°C
0.092
Atrazine
-
A216S/T217D/T219V/A220H/D250G, site-directed mutagenesis, AtzA-variant 297, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.092
Atrazine
-
A216Y/T217D/T219Y/A220H/D250V, site-directed mutagenesis, AtzA-variant 422, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.092
Atrazine
-
A216S/T217D/T219V/A220H/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
0.092
Atrazine
-
A216Y/T217D/T219Y/A220H/D250V, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
0.093
Atrazine
-
A216Y/T217D/T219T/A220H/D250E, site-directed mutagenesis, AtzA best variant consensus, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.093
Atrazine
-
A216Y/T217D/A220H/D250E, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
0.095
Atrazine
-
A216G/T217D/T219A/A220V/D250W, site-directed mutagenesis, AtzA-variant 305, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.095
Atrazine
-
A216G/T217D/T219A/A220V/D250W, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
0.1
Atrazine
-
A216H/T217A/T219E/A220S/D250S, site-directed mutagenesis, AtzA-variant 662, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.1
Atrazine
-
A216H/T217A/T219E/A220S/D250S, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
0.105
Atrazine
-
A216S/T217D/T219G/A220S/D250D, site-directed mutagenesis, AtzA-variant 841, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.105
Atrazine
-
A216S/T217D/T219G/A220S, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
0.11
Atrazine
-
D30G/Q91M/T195A/N429S/M99T/R290H, pH 7.2, 23°C
0.131
Atrazine
-
Q71P/D128Y/I194V/T195A/M315I/R389C/H399Q/A470T, pH 7.2, 23°C
0.132
Atrazine
-
V12C/A139P/M315I/R389C/I393E/L395R/F439L, pH 7.2, 23°C
0.138
Atrazine
-
D30G/Q71P/R271C/L288Q/M337T/R389C/H399Q/N429S, pH 7.2, 23°C
0.14
Atrazine
-
V12T/I393G/R389C/L395W/N429S/L446S/V466A, pH 7.2, 23°C
0.142
Atrazine
-
V12A/Q71T/T121A/A173V/M315I/H399Q/N429S/V466A, pH 7.2, 23°C
0.145
Atrazine
-
V12A/Q71T/A173V/M315I/H399Q/N429S/V466A, pH 7.2, 23°C
0.146
Atrazine
recombinant wild-type enzyme, pH 7.2, 25°C
0.148
Atrazine
-
D30G/G147D/G162E/A170V/H406P/V466A, pH 7.2, 23°C
0.15
Atrazine
-
V12A/Q71T/M315I/H399Q/N429S/V466A, pH 7.2, 23°C
0.15
Atrazine
-
wild-type enzyme, pH 7.2, 23°C
0.153
Atrazine
-
more than 0.153 mM. AtzA wild type, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
0.153
Atrazine
-
AtzA wild-type, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
0.9
Atrazine
-
A216G/T217D/T219G/A220H/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
3.1
Atrazine
-
mutant E241Q, pH and temperature not specified in the publication
13.3
Atrazine
-
mutant R325S, pH and temperature not specified in the publication
19
Atrazine
-
wild-type enzyme, pH 7.0, temperature not specified in the publication
additional information
additional information
-
reduction in Km observed in the AtzA variants has allowed the full kinetic profile for the AtzA-catalyzed dechlorination of atrazine to be determined for the first time, revealing the hitherto-unreported substrate cooperativity in AtzA
-
additional information
additional information
kinetic parameters of diverse mutants relative to the wild-type values, overview
-
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0.8
2,4-diisopropylamino-6-hydroxy-1,3,5-triazine
-
deamination
3.2
2-(N-ethylamino)-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine
-
deamination
1.6
2-chloro-4-(N-ethylamino)-6-hydroxy-1,3,5-triazine
-
dechlorination
1.9
2-chloro-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine
-
dechlorination
1.4
6-hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-triazine
-
deamination
0.467
ametryn
-
mutant R325S, pH and temperature not specified in the publication
6.04
ametryn
-
wild-type enzyme, pH 7.0, temperature not specified in the publication
0.0869
Atrazine
-
mutant R325S, pH and temperature not specified in the publication
0.137
Atrazine
-
mutant E241Q, pH and temperature not specified in the publication
1.49
Atrazine
-
wild-type enzyme, pH 7.0, temperature not specified in the publication
1.6
Atrazine
recombinant wild-type enzyme, pH 7.2, 25°C
1.66
Atrazine
-
wild-type enzyme, pH 7.2, 23°C
1.67
Atrazine
-
D30G/Q91M/T195A/N429S/M99T/R290H, pH 7.2, 23°C
2.2
Atrazine
-
more than 0.153 mM. AtzA wild type, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
2.2
Atrazine
-
AtzA wild-type, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
2.3
Atrazine
-
A216S/T217A/T219P/A220F/D250G, site-directed mutagenesis, AtzA-variant 357, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
2.3
Atrazine
-
A216S/T217A/T219P/A220F/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
2.87
Atrazine
-
Q71R/V58A/R389C/I209M/E317G, pH 7.2, 23°C
3.81
Atrazine
-
V12C/A139P/M315I/R389C/I393E/L395R/F439L, pH 7.2, 23°C
3.86
Atrazine
-
Q71P/D128Y/I194V/T195A/M315I/R389C/H399Q/A470T, pH 7.2, 23°C
4.06
Atrazine
-
D30G/Q71P/R271C/L288Q/M337T/R389C/H399Q/N429S, pH 7.2, 23°C
4.28
Atrazine
-
V12A/Q71T/A173V/M315I/H399Q/N429S/V466A, pH 7.2, 23°C
4.3
Atrazine
-
A216A/T217D/T219E/A220A/D250D, site-directed mutagenesis, AtzA-variant 288, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
4.3
Atrazine
-
T217D/T219E, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
4.32
Atrazine
-
V12A/Q71T/M315I/H399Q/N429S/V466A, pH 7.2, 23°C
4.73
Atrazine
-
V12A/Q71T/T121A/A173V/M315I/H399Q/N429S/V466A, pH 7.2, 23°C
4.87
Atrazine
-
D30G/G147D/G162E/A170V/H406P/V466A, pH 7.2, 23°C
5.86
Atrazine
-
V12T/I393G/R389C/L395W/N429S/L446S/V466A, pH 7.2, 23°C
6.2
Atrazine
-
A216G/T217D/T219A/A220V/D250W, site-directed mutagenesis, AtzA-variant 305, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
6.2
Atrazine
-
A216G/T217D/T219A/A220V/D250W, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
6.5
Atrazine
-
A216Y/T217D/T219Y/A220H/D250V, site-directed mutagenesis, AtzA-variant 422, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
6.5
Atrazine
-
A216Y/T217D/T219Y/A220H/D250V, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
6.8
Atrazine
-
A216S/T217D/T219V/A220H/D250G, site-directed mutagenesis, AtzA-variant 297, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
6.8
Atrazine
-
A216S/T217D/T219V/A220H/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
7.4
Atrazine
-
A216H/T217A/T219E/A220S/D250S, site-directed mutagenesis, AtzA-variant 662, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
7.4
Atrazine
-
A216H/T217A/T219E/A220S/D250S, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
8
Atrazine
-
A216A/T217S/T219H/A220G/D250Y, site-directed mutagenesis, AtzA-variant 431, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
8
Atrazine
-
T217S/T219H/A220G/D250Y, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
8.5
Atrazine
-
A216S/T217D/T219G/A220S/D250D, site-directed mutagenesis, AtzA-variant 841, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
8.5
Atrazine
-
A216S/T217D/T219G/A220S, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
12.7
Atrazine
-
A216G/T217D/T219G/A220H/D250G, site-directed mutagenesis, AtzA-variant 430, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
12.7
Atrazine
-
A216G/T217D/T219G/A220H/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
15.1
Atrazine
-
A216G/T217D/T219G/A220H/D250D, site-directed mutagenesis, AtzA-variant 734, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
15.1
Atrazine
-
A216G/T217D/T219G/A220H/D250D, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
27.9
Atrazine
-
A216Y/T217D/T219T/A220H/D250E, site-directed mutagenesis, AtzA best variant consensus, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme
27.9
Atrazine
-
A216Y/T217D/A220H/D250E, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm
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evolution
-
TrzN uniquely positions threonine 325 in place of a conserved aspartate that ligates the metal in most mononuclear amidohydrolases superfamily members
evolution
both enzyme AtzA and the alternative chlorohydrolase TrzN from Arthrobacter aurescens belong to the same large family of amidohydrolases, although they are so different physically and phylogenetically that it is likely that atrazine chlorohydrolase activity evolved independently in each enzyme, comparison of enzyme features, overview. In contrast to most other known hydrolytic dehalogenases, which use an active-site carboxylic acid (Asp) to displace the halide ion, the metal-dependent reaction mechanisms of AtzA and TrzN make these two enzyme lineages somewhat unusual in nature
evolution
-
TrzN uniquely positions threonine 325 in place of a conserved aspartate that ligates the metal in most mononuclear amidohydrolases superfamily members
-
metabolism
the enzyme catalyzes the first and necessary step in the breakdown of atrazine by the soil organism Pseudomonas sp. strain ADP
metabolism
the enzyme is critical in the atrazine degradation pathway
physiological function
-
atrazine chlorohydrolase 2 initiates bacterial metabolism of the herbicide atrazine by hydrolytic displacement of a chlorine substituent from the s-triazine ring
physiological function
Pseudomonas sp. strain ADP completely biodegrades atrazine to carbon dioxide and ammonia through the consecutive action of six catabolic enzymes, encoded by atzABCDEF, located on a selftransmissible plasmid, pADP-1. The first reaction is initiated by the enzyme AtzA, resulting in the dechlorination of atrazine to yield hydroxyatrazine, which is non-herbicidal and non-phytotoxic
physiological function
the enzyme catalyzes dechlorination of atrazine
physiological function
the enzyme is involved in mineralization of atrazine
physiological function
-
atrazine chlorohydrolase 2 initiates bacterial metabolism of the herbicide atrazine by hydrolytic displacement of a chlorine substituent from the s-triazine ring
-
additional information
-
development of fiber-optic biosensors for detection of atrazine using the atrazine chlorohydrolase, quantification of hydrochloric acid release, optimization, overview
additional information
Clavibacter michiganese
-
development of fiber-optic biosensors for detection of atrazine using the atrazine chlorohydrolase, quantification of hydrochloric acid release, optimization, overview
additional information
enzyme active site structure, overview. The channel, substrate-binding pocket and active site are comprised of His66, His68, Gln71, Phe84, Tyr85, Trp87, Leu88, Phe89, Val92, Tyr93, Asp128, Met155, Phe157, Met160, Asp161, Ile164, Gln165, Val168, Leu180, Ser182, Ile183, Met184, Ala216, Thr217, Thr219, Ala220, His243, Glu246, Asp250, His276, Leu305, Asp327, Asn328 and Ser331. Structure comparison of AtzA and the alternative chlorohydrolase TrzN from Arthrobacter aurescens, overview
additional information
-
enzyme active site structure, overview. The channel, substrate-binding pocket and active site are comprised of His66, His68, Gln71, Phe84, Tyr85, Trp87, Leu88, Phe89, Val92, Tyr93, Asp128, Met155, Phe157, Met160, Asp161, Ile164, Gln165, Val168, Leu180, Ser182, Ile183, Met184, Ala216, Thr217, Thr219, Ala220, His243, Glu246, Asp250, His276, Leu305, Asp327, Asn328 and Ser331. Structure comparison of AtzA and the alternative chlorohydrolase TrzN from Arthrobacter aurescens, overview
additional information
-
homology model of the AtzA wild-type enzyme and mutant enzymes. Only five of the seven substitutions (V92L, M155V, M256I, Y261S and A296T) can be accurately located using the homology model, the remaining two (A170T and P258T) lying in regions of primary structure that can not be accurately mapped to the template used in the model (a protein of unknown function from Thermotoga maritima; PDB: 1J6P)
additional information
homology modeling of enzyme AtzA, structure modeling and distribution of substitution sites
additional information
Clavibacter michiganese ATZ1
-
development of fiber-optic biosensors for detection of atrazine using the atrazine chlorohydrolase, quantification of hydrochloric acid release, optimization, overview
-
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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
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AtzA mutant
A216S/T217D/T219G/A220S
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AtzA mutant
A216S/T217D/T219V/A220H/D250G
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AtzA mutant
A216Y/T217D/A220H/D250E
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AtzA mutant
A216Y/T217D/T219Y/A220H/D250V
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AtzA mutant
T217D/T219E
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AtzA mutant
T217S/T219H/A220G/D250Y
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AtzA mutant
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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