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Literature summary for 1.11.1.6 extracted from

  • Shin, D.H.; Choi, Y.S.; Cho, Y.H.
    Unusual properties of catalase A (KatA) of Pseudomonas aeruginosa PA14 are associated with its biofilm peroxide resistance (2008), J. Bacteriol., 190, 2663-2670.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information switch of the coding region for KatA enzyme with those for KatA from Bacillus subtilis and CatA from Streptomyces coelicolor, and expression of the catalases under the potential katA-regulatory elements in Pseudomonas aeruginosa. Activities of the Bacillus subtilis and Streptomyces coelicolor enzymes are less than 40% of the native Pseudomonmas enzyme activity. Bacillus subtilis and Streptomyces coelicolor enzymes are rather susceptible to proteinase K, whereas the Pseudomonas enzyme is highly stable against proteinase K. Bacillus subtilis and Streptomyces coelicolor enzymes are not detectable in the extracellular milieu, but they fully rescue the peroxide sensitivity and osmosensitivity of the Pseudomonas katA mutant, respectively, as well as the attenuated virulence of the katA mutant in mouse acute infection and Drosophila melanogaster models. However, neither enzyme rescues the peroxide susceptibility of the katA mutant in a biofilm growth state Pseudomonas aeruginosa PA14
additional information switch of the coding region for Pseudomonas aeruginosa KatA enzyme with those for CatA from Streptomyces coelicolor and expression of the catalases under the potential katA-regulatory elements in Pseudomonas aeruginosa. Activitiy of the Streptomyces coelicolor enzyme is less than 40% of the native Pseudomomas enzyme activity. Streptomyces coelicolor enzyme is rather susceptible to proteinase K, whereas the Pseudomonas enzyme is highly stable against proteinase K. Streptomyces coelicolor enzyme is not detectable in the extracellular milieu, but it fully rescues the peroxide sensitivity and osmosensitivity of the Pseudomonas katA mutant, as well as the attenuated virulence of the katA mutant in mouse acute infection and Drosophila melanogaster models. However, it does not rescue the peroxide susceptibility of the katA mutant in a biofilm growth state Streptomyces coelicolor
additional information switch of the coding region for Pseudomonas aeruginosa KatA enzyme with those for KatA from Bacillus subtilis, and expression of the catalases under the potential katA-regulatory elements in Pseudomonas aeruginosa. Activitiy of the Bacillus subtilis enzyme is less than 40% of the native Pseudomonas enzyme activity. Bacillus subtilis enzyme is rather susceptible to proteinase K, whereas the Pseudomonas enzyme is highly stable against proteinase K. Bacillus subtilis enzyme is not detectable in the extracellular milieu, but it fully rescues the peroxide sensitivity and osmosensitivity of the Pseudomonas katA mutant, as well as the attenuated virulence of the katA mutant in mouse acute infection and Drosophila melanogaster models. However, it does not rescue the peroxide susceptibility of the katA mutant in a biofilm growth state Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
KatA
-
Bacillus subtilis KatA
-
KatA
-
Pseudomonas aeruginosa PA14
-
KatA
-
Pseudomonas aeruginosa PA14 KatA
-
KatA
-
Streptomyces coelicolor
-
CatA
-