Protein Variants | Comment | Organism |
---|---|---|
W107F | mutation in key distal side residue, disrupts high-affinity binding of substrate isonicotinic hydrazide | Mycobacterium tuberculosis |
Y229F | mutation in key distal side residue, disrupts high-affinity binding of substrate isonicotinic hydrazide | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
bifunctional catalase-peroxidase KatG | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-H-pyrrol-2-carbohydrazide | analysis of association and dissociation rate constants | Mycobacterium tuberculosis | ? | - |
? | |
benzoic hydrazide | analysis of association and dissociation rate constants | Mycobacterium tuberculosis | ? | - |
? | |
furoic hydrazide | analysis of association and dissociation rate constants | Mycobacterium tuberculosis | ? | - |
? | |
isonicotinic hydrazide | antituberculosis drug, bactericidal function neeeds activation by bifunctional catalase-peroxidase KatG to produce an acyl-NAD adduct. Substrate binds with high affinity to a small portion of ferric enzyme in a six-coordinate heme iron form | Mycobacterium tuberculosis | ? | - |
? | |
nicotinic hydrazide | analysis of association and dissociation rate constants | Mycobacterium tuberculosis | ? | - |
? | |
picolinic hydrazide | analysis of association and dissociation rate constants | Mycobacterium tuberculosis | ? | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | substrate isonicotinic hydrazide binds with high affinity to a small protion of ferric enzyme in a six-coordinate heme iron form, binding is associated with a large enthalpie loss. Binding parameters do not depend on pH in the range of pH 5-8 | Mycobacterium tuberculosis |