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Literature summary for 1.11.1.6 extracted from

  • Zhao, X.; Yu, S.; Magliozzo, R.S.
    Characterization of the binding of isoniazid and analogues to Mycobacterium tuberculosis catalase-peroxidase (2007), Biochemistry, 46, 3161-3170.
    View publication on PubMed

Protein Variants

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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
bifunctional catalase-peroxidase KatG
-

Substrates and Products (Substrate)

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

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