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Information on EC 3.8.1.8 - atrazine chlorohydrolase and Organism(s) Pseudomonas sp. and UniProt Accession P72156
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3.8.1.8 atrazine chlorohydrolaseIUBMB Comments
Involved in the degradation of the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, in bacteria.
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Word Map
- 3.8.1.8
-
herbicide
- adp
-
dechlorination
- hydroxyatrazine
- arthrobacter
- s-triazine
-
amidohydrolase
- nocardioides
- melamine
-
atrazine-degrading
-
bioremediation
- agriculture
- haematococcus
- ametryn
-
cyanuric
- aurescens
-
phytoremediation
- analysis
- environmental protection
- biotechnology
The taxonomic range for the selected organisms is: Pseudomonas sp.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
atrazine chlorohydrolase, triazine hydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
atrazine dechlorinase
-
-
-
-
dechlorinase, atrazine (9CI)
-
-
-
-
additional information
-
enzyme shows 98% amino acid sequence identitiy with melamine deaminase from Pseudomonas sp. strain NRRL B-12227, but does not catalyse the same reaction
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
atrazine + H2O = hydroxyatrazine + chloride
two plausible reaction mechanisms are proposed involving either bidentate (a) or mondentate (b) coordination of the atrazine Cl atom to the Fe2+ centre of the AtzA active site, comparisons, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -
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
168680-16-8
-
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
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
-
-
-
-
?
atrazine + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + chloride
-
-
-
-
?
atrazine with Cl to F exchange + H2O
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + HF
-
-
-
-
?
desethylatrazine + H2O
2-hydroxy-4-amino-6-(isopropylamino)-1,3,5-triazine + HCl
-
-
-
-
?
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
-
-
-
-
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
-
-
?
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
-
-
?
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
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
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
the AtzA hexamer contains one essential Fe2+ per monomer and active site
Fe2+
-
iron containing metalloenzyme, 1:1 metal to subunit stoichiometry, bound at the active site, activates
additional information
additional information
-
no metal ions detectable with the enzym expressed in E. coli
additional information
-
influence of and reconstitution with metals Mn2+, Fe2+, and Co2+, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
complete inhibition, reversible by addition of Fe2+, Mn2+, or Co2+
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+
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
LITERATURE
IMAGE
0.02
2-(N-ethylamino)-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine
-
deamination
0.04
6-hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-triazine
-
deamination
additional information
additional information
kinetic parameters of diverse mutants relative to the wild-type values, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
2-(N-ethylamino)-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine
-
deamination
1.4
6-hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-triazine
-
deamination
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.6
purified recombinant wild-type enzyme, 0.046 mM atrazine, pH 7.2, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
physiological function
additional information
metabolism
the enzyme catalyzes the first and necessary step in the breakdown of atrazine by the soil organism Pseudomonas sp. strain ADP
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
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 modeling of enzyme AtzA, structure modeling and distribution of substitution sites
additional information
-
development of fiber-optic biosensors for detection of atrazine using the atrazine chlorohydrolase, quantification of hydrochloric acid release, optimization, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
the AtzA hexamer is a trimer of dimers, (alphabeta)3, the dimer interface is significantly larger than the individual protomer interfaces used to make up the hexamer, three-dimensional structure analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 8°C, resulting in two different crystal forms, X-ray diffraction structure determination and analysis at 2.8 A and 2.2 A resolution, respectively, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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, 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, 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
expression of holoenzyme and subfragment with catalytic activity in Escherichia coli DH5-alpha
-
using the vectors pACYC184 and pMD4 for expression in Escherichia coli DH5alpha cells
-
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
LITERATURE
environmental protection
bioremidiation, use of enhanced expression of a modified bacterial atrazine chlorohydrolase, p-AtzA, in transgenic grasses, tall fescue or Festuca arundinacea, ryegrass or Lolium perenne, and switchgrass or Panicum virgatum, and the legume alfalfa, Medicago sativa, for the biodegradation of atrazine
agriculture
analysis
-
fiber-optic biosensors for detection of atrazine at low concentrations in soil using the atrazine chlorohydrolase and quantification of hydrochloric acid release, optimization, overview
agriculture
-
atrazine metabolites, i.e. alkylamines, are toxic in higher concentrations for the bacteria without buffered milieu due to low pH
agriculture
-
degradation of chemically stable and toxic herbicide atrazine in soil and groundwater to non-toxic hydroxyatrazine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
De Souza, M.L.; Wackett, L.P.; Boundy-Mills, K.L.; Mandelbaum, R.T.; Sadowsky, M.J.
Cloning, characterization, and expression of a gene region from Pseudomonas sp. strain ADP involved in the dechlorination of atrazine
Appl. Environ. Microbiol.
61
3373-3378
1995
Pseudomonas sp.
De Souza, M.L.; Sadowsky, M.J.; Wackett, L.P.
Atrazine chlorohydrolase from Pseudomonas sp. strain ADP: gene sequence, enzyme purification, and protein characterization
J. Bacteriol.
178
4894-4900
1996
Pseudomonas sp.
De Souza, M.L.; Newcombe, D.; Alvey, S.; Crowley, D.E.; Hay, A.; Sadowsky, M.J.; Wackett, L.P.
Molecular basis of a bacterial consortium: interspecies catabolism of atrazine
Appl. Environ. Microbiol.
64
178-184
1998
Clavibacter michiganese, Clavibacter michiganese ATZ1, Pseudomonas sp.
De Souza, M.L.; Seffernick, J.; Martinez, B.; Sadowsky, M.J.; Wackett, L.P.
The atrazine catabolism genes atzABC are widespread and highly conserved
J. Bacteriol.
180
1951-1954
1998
Agrobacterium tumefaciens, Agrobacterium tumefaciens J14a, Alcaligenes sp., Alcaligenes sp. SG1, Pseudomonas sp., Ralstonia sp., Ralstonia sp. M91-3
Seffernick, J.; Johnson, G.; Sadowsky, M.J.; Wackett, L.P.
Substrate specificity of atrazine chlorohydrolase and atrazine-catabolizing bacteria
Appl. Environ. Microbiol.
66
4247-4252
2000
Agrobacterium tumefaciens, Agrobacterium tumefaciens J14a, Alcaligenes sp., Alcaligenes sp. SG1, Clavibacter michiganese, Clavibacter michiganese ATZ1, Pseudomonas sp., Ralstonia pickettii, Ralstonia pickettii D, Rhizobium sp., Rhizobium sp. PATR
Seffernick, J.L.; McTavish, H.; Osborne, J.P.; de Souza, M.L.; Sadowsky, M.J.; Wackett, L.P.
Atrazine chlorohydrolase from Pseudomonas sp. strain ADP is a metalloenzyme
Biochemistry
41
14430-14437
2002
Pseudomonas sp.
Seffernick, J.L.; de Souza, M.L.; Sadowsky, M.J.; Wackett, L.P.
Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionally different
J. Bacteriol.
183
2405-2410
2001
Pseudomonas sp.
Kersante, A.; Martin-Laurent, F.; Soulas, G.; Binet, F.
Interactions of earthworms with Atrazine-degrading bacteria in an agricultural soil
FEMS Microbiol. Ecol.
57
192-205
2006
Pseudomonas sp.
Seffernick, J.L.; Aleem, A.; Osborne, J.P.; Johnson, G.; Sadowsky, M.J.; Wackett, L.P.
Hydroxyatrazine N-ethylaminohydrolase (AtzB): an amidohydrolase superfamily enzyme catalyzing deamination and dechlorination
J. Bacteriol.
189
6989-6997
2007
Pseudomonas sp.
Das, N.; Reardon, K.
Fiber-optic biosensor for the detection of atrazine: characterization and continuous measurements
Anal. Lett.
45
251-261
2012
Clavibacter michiganese, Clavibacter michiganese ATZ1, Pseudomonas sp.
-
Wang, H.; Chen, X.; Xing, X.; Hao, X.; Chen, D.
Transgenic tobacco plants expressing atzA exhibit resistance and strong ability to degrade atrazine
Plant Cell Rep.
29
1391-1399
2010
Arthrobacter sp. (Q8GG87), Arthrobacter sp. AD1 (Q8GG87), Pseudomonas sp. (P72156)
Peat, T.S.; Newman, J.; Balotra, S.; Lucent, D.; Warden, A.C.; Scott, C.
The structure of the hexameric atrazine chlorohydrolase AtzA
Acta Crystallogr. Sect. D
71
710-720
2015
Pseudomonas sp. (P72156), Pseudomonas sp.
Wang, Y.; Li, X.; Chen, X.; Chen, D.
Directed evolution and characterization of atrazine chlorohydrolase variants with enhanced activity
Biochemistry (Moscow)
78
1104-1111
2013
Pseudomonas sp. (P72156)
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Release 2023.1 (January 2023)
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