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Literature summary for 1.11.1.6 extracted from

  • Charalabous, P.; Risk, J.M.; Jenkins, R.; Birss, A.J.; Hart, C.A.; Smalley, J.W.
    Characterization of a bifunctional catalase-peroxidase of Burkholderia cenocepacia (2007), FEMS Immunol. Med. Microbiol., 50, 37-44.
    View publication on PubMed
Search for more literature for 1.11.1.6

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Burkholderia cenocepacia

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibited by exposure of cells to 3-amino-1,2,4-triazole Burkholderia cenocepacia

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
 x * 97000, SDS-PAGE of mature enzyme, x * 80000, SDS-PAGE of recombinant protein Burkholderia cenocepacia
97000
-
 x * 97000, SDS-PAGE of mature enzyme, x * 80000, SDS-PAGE of recombinant protein Burkholderia cenocepacia

Organism

Organism UniProt Comment Textmining
Burkholderia cenocepacia Q4F6N6 bifunctional catalase-peroxidase KatG
-

Subunits

Subunits Comment Organism
? x * 97000, SDS-PAGE of mature enzyme, x * 80000, SDS-PAGE of recombinant protein Burkholderia cenocepacia

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 6 both catalase and peroxidase activity Burkholderia cenocepacia

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 no catalytic activity at pH 9.0 Burkholderia cenocepacia
5.5 8.5
-
 Burkholderia cenocepacia