Information on EC 3.8.1.8 - atrazine chlorohydrolase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
3.8.1.8
-
RECOMMENDED NAME
GeneOntology No.
atrazine chlorohydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
atrazine + H2O = 4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
dechlorination
hydrolysis
hydrolysis of C-halide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Atrazine degradation
-
-
atrazine degradation I (aerobic)
-
-
atrazine degradation III
-
-
degradation of aromatic, nitrogen containing compounds
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
atrazine chlorohydrolase
Involved in the degradation of the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, in bacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
168680-16-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain J14a
-
-
Manually annotated by BRENDA team
strain ST96-4 containing plasmid pADP1::Tn5
-
-
Manually annotated by BRENDA team
strain SG1
-
-
Manually annotated by BRENDA team
strain SG1
-
-
Manually annotated by BRENDA team
Arthrobacter aurescens
gene trzN
-
-
Manually annotated by BRENDA team
Arthrobacter aurescens TC1
gene trzN
-
-
Manually annotated by BRENDA team
Arthrobacter nicotinovorans
strain HIM
-
-
Manually annotated by BRENDA team
Arthrobacter nicotinovorans HIM
strain HIM
-
-
Manually annotated by BRENDA team
gene atzA
UniProt
Manually annotated by BRENDA team
Clavibacter michiganese
Clavibacter michiganese ATZ1
JM109
-
-
Manually annotated by BRENDA team
JM109
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain C190
-
-
Manually annotated by BRENDA team
strain C190
-
-
Manually annotated by BRENDA team
D
-
-
Manually annotated by BRENDA team
strain M91-3
-
-
Manually annotated by BRENDA team
strain M91-3
-
-
Manually annotated by BRENDA team
strain PATR
-
-
Manually annotated by BRENDA team
strain PATR
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-di(N-isobutylamino)-6-hydroxy-1,3,5-triazine + H2O
6-[(2-methylpropyl)amino]-1,3,5-triazine-2,4-diol + isobutylamine
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
2,4-di(N-tertbutylamino)-6-hydroxy-1,3,5-triazine + H2O
6-(tert-butylamino)-1,3,5-triazine-2,4-diol + tert-butylamine
show the reaction diagram
-
-
-
-
?
2,4-diamino-6-hydroxy-1,3,5-triazine + H2O
6-amino-1,3,5-triazine-2,4-diol + NH3
show the reaction diagram
-
-
-
-
?
2,4-diethylamino-6-hydroxy-1,3,5-triazine + H2O
6-(methylamino)-1,3,5-triazine-2,4-diol + ethylamine
show the reaction diagram
-
-
-
-
?
2,4-diisopropylamino-6-hydroxy-1,3,5-triazine + H2O
6-[(1-methylethyl)amino]-1,3,5-triazine-2,4-diol + propan-2-amine
show the reaction diagram
-
-
-
-
?
2,4-dimethylamino-6-hydroxy-1,3,5-triazine + H2O
6-(methylamino)-1,3,5-triazine-2,4-diol + methylamine
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
2-amino-4-chloro-6-hydroxy-1,3,5-triazine + H2O
6-amino-1,3,5-triazine-2,4-diol + Cl-
show the reaction diagram
-
-
-
-
?
2-amino-4-hydroxy-6-(N-hydroxyethylamino)-1,3,5-triazine + H2O
6-[(2-hydroxyethyl)amino]-1,3,5-triazine-2,4-diol + NH3
show the reaction diagram
-
-
-
-
?
2-amino-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine + H2O
6-(isopropylamino)-1,3,5-triazine-2,4-diol + NH3
show the reaction diagram
-
-
-
-
?
2-amino-6-(N-ethylamino)-4-hydroxy-1,3,5-triazine + H2O
6-(ethylamino)-1,3,5-triazine-2,4-diol + NH3
show the reaction diagram
-
-
-
-
?
2-chloro-4-(N-ethylamino)-6-hydroxy-1,3,5-triazine + H2O
6-(ethylamino)-1,3,5-triazine-2,4-diol + Cl-
show the reaction diagram
-
-
-
-
?
2-chloro-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine + H2O
6-(isopropylamino)-1,3,5-triazine-2,4-diol + Cl-
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
2-hydroxy-4-(N-isopropylamino)-6-(N-(3-methoxypropyl)amino)-1,3,5-triazine + H2O
?
show the reaction diagram
-
-
-
-
?
6-(ethylamino)-4-(methylamino)-1,3,5-triazin-2-ol + H2O
6-(ethylamino)-1,3,5-triazine-2,4-diol + methylamine
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
ametryn + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + H-S-CH3
show the reaction diagram
atratone + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + methanol
show the reaction diagram
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
show the reaction diagram
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
show the reaction diagram
atrazine + H2O
cyanuric acid + ?
show the reaction diagram
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
show the reaction diagram
cyanazine + H2O
2-{[4-(ethylamino)-6-hydroxy-1,3,5-triazin-2-yl]amino}-2-methylpropanenitrile + HCl
show the reaction diagram
desethylatrazine + H2O
2-hydroxy-4-amino-6-(isopropylamino)-1,3,5-triazine + HCl
show the reaction diagram
hydroxyatrazine + H2O
N-isopropylammelide + ethylamine
show the reaction diagram
-
-
-
-
?
prometryn + H2O
?
show the reaction diagram
propazine + H2O
4,6-bis(propan-2-ylamino)-1,3,5-triazin-2-ol + HCl
show the reaction diagram
simazine + H2O
4,6-diethylamino-1,3,5-triazine + HCl
show the reaction diagram
terbuthylazine + H2O
?
show the reaction diagram
Arthrobacter nicotinovorans
-
-
-
-
?
atrazine + H2O
additional information
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
show the reaction diagram
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HCl
show the reaction diagram
hydroxyatrazine + H2O
N-isopropylammelide + ethylamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activates
Mn2+
-
slightly stimulating
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
complete inhibition, reversible by addition of Fe2+, Mn2+, or Co2+
aminotriazine
-
-
Cu2+
-
complete inhibition, not due to displacement of the native active site metal ion Fe2+
Fe3+
-
complete inhibition, not due to displacement of the native active site metal ion Fe2+
Ni2+
-
complete inhibition, not due to displacement of the native active site metal ion Fe2+
oxalic acid
-
reversible by addition of Fe2+, Mn2+, or Co2+
Zn2+
-
complete inhibition, not due to displacement of the native active site metal ion Fe2+
additional information
-
no inhibition by melamine and 2-chloro-4,6-diamino-S-triazine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
3.9 - 7.8
ametryn
0.0238 - 19
Atrazine
0.02
hydroxyatrazine
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
2,4-diisopropylamino-6-hydroxy-1,3,5-triazine
Pseudomonas sp.
-
deamination
3.2
2-(N-ethylamino)-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine
Pseudomonas sp.
-
deamination
1.6
2-chloro-4-(N-ethylamino)-6-hydroxy-1,3,5-triazine
Pseudomonas sp.
-
dechlorination
1.9
2-chloro-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine
Pseudomonas sp.
-
dechlorination
1.4
6-hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-triazine
Pseudomonas sp.
-
deamination
0.467 - 6.04
ametryn
0.0869 - 27.9
Atrazine
3
hydroxyatrazine
Pseudomonas sp.
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
60 - 1530
ametryn
6.5 - 78
Atrazine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0001
Clavibacter michiganese
-
crude cell extract
0.0017
-
crude cell extract
0.0039
-
crude cell extract
0.0045
-
crude cell extract
0.0048
-
crude cell extract
0.0074
-
crude cell extract
0.0162
-
partially purified enzyme
0.16
-
crude extract
0.33
-
prurification step ammonium sulfate precipitation
1.05
-
prurification step ceramic hydroxyapatite type I column
2.6
-
purified recombinant wild-type enzyme, 0.046 mM atrazine, pH 7.2, 25C
3.7
-
about, purified recombinant enzyme
4.5
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
Arthrobacter aurescens
-
mutant E241Q
7.2
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 55
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Arthrobacter aurescens
Arthrobacter aurescens
Pseudomonas sp. (strain ADP)
Pseudomonas sp. (strain ADP)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
subunit molecular mass, determind by SDS-Page
54000
-
determined by SDS-PAGE
105000
-
holoenzyme molecular mass, determind by gel-filtration
200000
-
about, non-denaturating PAGE
245000
-
gel filtration
315000
-
hexameric recombinant detagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homodimer
pentamer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant Zn2+-bound wild-type TrzN, and zinc-bound TrzN mutant E241Q complexed with ametryn or atratone, hanging drop method, for the wild-typeenzyme: 21 mg/ml TrzN in 25 mM MOPS, pH 5.5, and 1mM ZnCl2 with precipitant solution containing 25% PEG 3350, 0.1 M Bis-Tris, pH 5.5, 0.2 M ammonium sulfate, and 1 mM ZnCl2, 7-8 days at 25C. For the mutant enzyme: 6.6 mg/ml TrzN-E241Q in 25 mM MOPS, pH 5.5, and 1 mM ZnCl2 with precipitant containing 30% PEG 4000, 0.1 M sodium citrate, pH 5.6, 0.2 M ammonium acetate, and 1 mM ZnCl2, 2 weeks at 25C, soaking of crystals for 1 h in cryobuffer composed of its mother liquid, 15% glycerol, and excess of the ametryn or atratone powder, X-ray diffraction structure determination and analysis at 1.40 A, 1.93 A, and 1.64 A resolutions, respectively, modeling
Arthrobacter aurescens
-
purified recombinant detagged wildtype and mutant enzymes, mixing of 11.6 mg/ml protein in 50 mM HEPES, pH 7.5, and 100 mM NaCl with a reservoir solution containing 5.5% w/v PEG 8000, 2.7% v/v diethylene glycol, 50 mM HEPES, pH 7.1 or 50 mM HEPES pH 7.3, 4.6% w/v PEG 10 000, at 8C, resulting in two different crystal forms, X-ray diffraction structure determination and analysis at 2.8 A and 2.2 A resolution, respectively, modeling
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by ammonium sulfate precipitation and filtration using 100 and 50 kDa cut-off membrane filters
-
partially purified
-
recombinant from Escherichia coli
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, tag cleavage by by thrombin proteolysis, and again gel filtration
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) solubilized from inclusion bodies by nickel affinity chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
Arthrobacter aurescens
-
using a CHT ceramic hydroxyapatite type I column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of holoenzyme and subfragment with catalytic activity in Escherichia coli DH5-alpha
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Arthrobacter aurescens
-
five amino acids within the substrate-binding pocket of AtzA are chosen for randomization yields one variant enzyme with 20fold-greater catalytic efficiency than that of wild-type AtzA
-
gene atzA, application of a Haematococcus pluvialis-based method to screen AtzA variants from a random mutagenesis library, genotyping, Haematococcus pluvialis strain H1 is used to test atrazine concentrations, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) in Inclusion bodies, subcloning in Escherichia coli strain DH5alpha-FT
-
gene atzA, DNA and amino acid sequence determination and analysis, genotyping of enzymes from eight triazine-degrading Aminobacter aminovorans strains isolated from French agricultural soils recurrently exposed to triazines in 2000. Subcloning in Escherichia coli strain JM109
-
gene atzA, expression in Nicotiana tabacum via Agrobacterium tumefaciens strain LBA4404-mediated transformation and expression under control of the CaMV 35S promoter, the transgenic tobacco lines expressing the wild-type atzA from Arthrobacter sp. strain AD1 show resistance to and a strong ability to degrade atrazine
gene atzA, expression in Nicotiana tabacum via Agrobacterium tumefaciens strain LBA4404-mediated transformation and expression under control of the CaMV 35S promoter, the transgenic tobacco lines expressing the wild-type atzA from Pseudomonas sp. strain ADP show resistance to and a strong ability to degrade atrazine
gene atzA, overexpression in Escherichia coli DH5alpha
-
gene atzA, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene atzA, transgenic expression in grasses, tall fescue, perennial ryegrass, and switchgrass, and the legume alfalfa or Medicago sativa, enhanced expression of p-AtzA is obtained by using combinations of the badnavirus promoter, the maize alcohol dehydrogenase first intron, and the maize ubiquitin promoter. For Medicago sativa, the first intron of the 5'-untranslated region tobacco alcohol dehydrogenase gene and the cassava vein mosaic virus promoter is used. Resistance of plants to atrazine in agar-based and hydroponic growth assays is correlated with in vivo levels of gene expression and atrazine degradation, trnasfection by Biolistic or by Agrobacterium tumefaciens methods, phenotypes, overview
-
using the vectors pACYC184 and pMD4 for expression in Escherichia coli DH5alpha cells
-
ENGINEERING
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
E241Q
Arthrobacter aurescens
-
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
Arthrobacter aurescens
-
site-directed mutagenesis, the mutation results in a 12fold decrease in kcat/Km, largely due to kcat
T325D
Arthrobacter aurescens
-
site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
T325E
Arthrobacter aurescens
-
site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
E241Q
Arthrobacter aurescens TC1
-
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
Arthrobacter aurescens TC1
-
site-directed mutagenesis, the mutation results in a 12fold decrease in kcat/Km, largely due to kcat
-
T325D
Arthrobacter aurescens TC1
-
site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
-
T325E
Arthrobacter aurescens TC1
-
site-directed mutagenesis, inactive active site mutant, altered active site structure compared to the wild-type enzyme
-
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
-
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
A170T/M256I/P258T/Y261S
-
commercially prepared mutant gene
-
H399Q
-
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
-
N429S
-
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
-
V12A
-
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
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
solubilization of recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) inclusion bodies
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
analysis
biotechnology
environmental protection