Protein Variants | Comment | Organism |
---|---|---|
S315T | most prevalent isonazid-resistant mutant, determination of Fe2+-binding/interaction structure, minimal alterations compared to the wild-type enzyme, mutant enzyme retains all active site properties for proper catalytic function | Mycobacterium tuberculosis |
S315T | isoniazid-resistant, mutant catalase-peroxidase retains all active site properties for proper catalytic function | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
CO | complexed with the enzyme, structure determination, binding kinetics | Mycobacterium tuberculosis | |
Fe2+ | wild-type and S315T mutant enzyme, determination of Fe2+-binding/interaction structure | Mycobacterium tuberculosis | |
NO | complexed with the enzyme, structure determination, binding kinetics | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
H2O2 | Mycobacterium tuberculosis | - |
O2 + H2O | - |
? | |
isoniazid + H2O2 | Mycobacterium tuberculosis | activation of antituberculosis drug isonazid, catalytic mechanism | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Mycobacterium tuberculosis | - |
enzyme KatG is a bifunctional | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 H2O2 = O2 + 2 H2O | catalytic mechanism | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
H2O2 | - |
Mycobacterium tuberculosis | O2 + H2O | - |
? | |
isoniazid + H2O2 | - |
Mycobacterium tuberculosis | ? | - |
? | |
isoniazid + H2O2 | activation of antituberculosis drug isonazid, catalytic mechanism | Mycobacterium tuberculosis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
catalase-peroxidase | - |
Mycobacterium tuberculosis |
catalase-peroxidase | bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7 | Mycobacterium tuberculosis |
KatG | - |
Mycobacterium tuberculosis |
KatG | bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7 | Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | wild-type and S315T mutant enzyme, determination of Fe2+-binding/interaction structure | Mycobacterium tuberculosis |