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Literature summary for 1.11.1.21 extracted from

  • Ivancich, A.; Donald, L.J.; Villanueva, J.; Wiseman, B.; Fita, I.; Loewen, P.C.
    Spectroscopic and kinetic investigation of the reactions of peroxyacetic acid with Burkholderia pseudomallei catalase-peroxidase, KatG (2013), Biochemistry, 52, 7271-7282.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Burkholderia pseudomallei

Organism

Organism UniProt Comment Textmining
Burkholderia pseudomallei
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peroxyacetic acid
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 Burkholderia pseudomallei ? in the absence of peroxidatic one-electron donors, the ferryl intermediates generated with a low excess of peroxyacetic acid slowly decay to the ferric resting state after several minutes. The Fe(IV)=O Trp330 radical cation, Fe(IV)=O Trp139 radical, and Fe(IV)=O Trp153 radical intermediates of the peroxidase-like cycle, formed with a low excess of peroxyacetic acid at low temperature, are also generated with a high excess of peroxyacetic acid at room temperature. Under high excess conditions, there is a rapid conversion to a persistent Fe(IV)=O intermediate. Specific tryptophan residues including W330, W139, and W153, methionine residues including Met264 of the M-Y-W adduct, and cysteine residues are either modified with one, two, or three oxygen atoms or cannot be identified in the spectrum because of other undetermined modifications. These oxidized residues are the source of electrons used to reduce the excess of peroxyacetic acid to acetic acid and return the enzyme to the ferric state ?