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Literature summary for 1.11.1.21 extracted from

  • Zhao, X.; Khajo, A.; Jarrett, S.; Suarez, J.; Levitsky, Y.; Burger, R.M.; Jarzecki, A.A.; Magliozzo, R.S.
    Specific function of the Met-Tyr-Trp adduct radical and residues Arg-418 and Asp-137 in the atypical catalase reaction of catalase-peroxidase KatG (2012), J. Biol. Chem., 287, 37057-37065.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
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 Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
D137S in the presence of H2O2, the adduct radical formed from covalently linked side chains of conserved amino acids Met255, Tyr229, and Trp107 is formed normally, but mutant is defective in forming dioxyheme and lacks catalase activity. Mutant exhibits a coincidence between adduct radical persistence and H2O2 consumption as a function of time, and enhanced subunit oligomerization during turnover Mycobacterium tuberculosis
R418L mutant is catalase deficient but exhibits normal formation of the adduct radical formed from covalently linked side chains of conserved amino acids Met255, Tyr229, and Trp107 and dioxyheme. Mutant exhibits a coincidence between adduct radical persistence and H2O2 consumption as a function of time, and enhanced subunit oligomerization during turnover Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information interaction between the side chain of residue Arg418 and Tyr229 in the adduct radical formed from covalently linked side chains of conserved amino acids Met255, Tyr229, and Trp107 favors reaction of the radical with the adjacent dioxyheme intermediate present throughout turnover. Release of molecular oxygen and regeneration of resting enzyme are thereby catalyzed in the last step of a proposed catalase reaction Mycobacterium tuberculosis ?
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