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Literature summary for 3.8.1.8 extracted from

  • Noor, S.; Changey, F.; Oakeshott, J.; Scott, C.; Martin-Laurent, F.
    Ongoing functional evolution of the bacterial atrazine chlorohydrolase AtzA (2014), Biodegradation, 25, 21-30.
    View publication on PubMed
Search for more literature for 3.8.1.8

Cloned(Commentary)

Cloned (Comment) Organism
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 Aminobacter aminovorans

Protein Variants

Protein Variants Comment Organism
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 Aminobacter aminovorans
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 Aminobacter aminovorans
M155V naturally occuring mutation A463G Aminobacter aminovorans
M256I/P258T/Y261S naturally occuring mutations G768C, C722A and A782C Aminobacter aminovorans
additional information 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 Aminobacter aminovorans
P258T naturally occuring mutation C722A Aminobacter aminovorans
V92L naturally occuring mutation G274T Aminobacter aminovorans
V92L/A170T/A296T naturally occuring mutations G274T, G508A, and G886A Aminobacter aminovorans

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required Aminobacter aminovorans

Organism

Organism UniProt Comment Textmining
Aminobacter aminovorans
-
-
-

Synonyms

Synonyms Comment Organism
AtzA
-
 Aminobacter aminovorans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Aminobacter aminovorans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.9
-
 assay at Aminobacter aminovorans

General Information

General Information Comment Organism
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) Aminobacter aminovorans