Cloned (Comment) | Organism |
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- |
Mycobacterium tuberculosis |
Protein Variants | Comment | Organism |
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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 | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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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 | ? | - |
? |