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Literature summary for 1.11.1.21 extracted from

  • Deemagarn, T.; Wiseman, B.; Carpena, X.; Ivancich, A.; Fita, I.; Loewen, P.C.
    Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei (2007), Proteins, 66, 219-228.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the D141E variant determined at 1.8 A resolution Burkholderia pseudomallei

Protein Variants

Protein Variants Comment Organism
D141A mutant with reduced catalase activity Burkholderia pseudomallei
D141E mutant with normal catalase activity but with modified kinetics Burkholderia pseudomallei
R108A mutant with reduced catalase activity Burkholderia pseudomallei
R108A/D141A activity is 18% lower than wild-type activity Burkholderia pseudomallei

Organism

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2 it is proposed that binding of substrate H2O2 to Asp141 and Arg108 controls H2O2 access to the heme active site, thereby modulating the catalase reaction Burkholderia pseudomallei O2 + H2O
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?

Synonyms

Synonyms Comment Organism
catalase -peroxidase KatG
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Burkholderia pseudomallei

Cofactor

Cofactor Comment Organism Structure
heme it is proposed that binding of substrate H2O2 to Asp141 and Arg108 controls H2O2 access to the heme active site, thereby modulating the catalase reaction Burkholderia pseudomallei