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Literature summary for 1.11.1.21 extracted from

  • Donald, L.J.; Krokhin, O.V.; Duckworth, H.W.; Wiseman, B.; Deemagarn, T.; Singh, R.; Switala, J.; Carpena, X.; Fita, I.; Loewen, P.C.
    Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry (2003), J. Biol. Chem., 278, 35687-35692.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
W111F site-directed mutagenesis, active site structure analysis Burkholderia pseudomallei

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ enzyme contains a heme modified with a special hydroperoxide group added to ring I Burkholderia pseudomallei

Organism

Organism UniProt Comment Textmining
Burkholderia pseudomallei
-
bifunctional catalase-peroxidase KatG
-

Reaction

Reaction Comment Organism Reaction ID
2 H2O2 = O2 + 2 H2O the catalytically relevant active site residues Trp111, Tyr238, and Met264 are linked by a covalent structure Burkholderia pseudomallei

Subunits

Subunits Comment Organism
More active site structure analysis of wild-type and mutant W111F enzymes Burkholderia pseudomallei

Synonyms

Synonyms Comment Organism
catalase-peroxidase
-
Burkholderia pseudomallei
KatG
-
Burkholderia pseudomallei