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Literature summary for 1.11.1.21 extracted from

  • Reyes, Y.I.A.; Janairo, G.C.; Franco, F.C.
    Theoretical insights on the binding of isoniazid to the active site residues of Mycobacterium tuberculosis catalase-peroxidase (2019), Tuberculosis, 114, 61-68 .
    View publication on PubMed
Search for more literature for 1.11.1.21

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the heme group Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 H2O2 Mycobacterium tuberculosis
-
 O2 + 2 H2O
-
 ?
2 H2O2 Mycobacterium tuberculosis H37Rv
-
 O2 + 2 H2O
-
 ?
2 H2O2 Mycobacterium tuberculosis ATCC 25618
-
 O2 + 2 H2O
-
 ?
isoniazid + H2O2 Mycobacterium tuberculosis pro-drug activation ?
-
 ?
isoniazid + H2O2 Mycobacterium tuberculosis H37Rv pro-drug activation ?
-
 ?
isoniazid + H2O2 Mycobacterium tuberculosis ATCC 25618 pro-drug activation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WIE5
-
-
Mycobacterium tuberculosis ATCC 25618 P9WIE5
-
-
Mycobacterium tuberculosis H37Rv P9WIE5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 H2O2
-
 Mycobacterium tuberculosis O2 + 2 H2O
-
 ?
2 H2O2
-
 Mycobacterium tuberculosis H37Rv O2 + 2 H2O
-
 ?
2 H2O2
-
 Mycobacterium tuberculosis ATCC 25618 O2 + 2 H2O
-
 ?
isoniazid + H2O2 pro-drug activation Mycobacterium tuberculosis ?
-
 ?
isoniazid + H2O2 i.e. isonicotinylhydrazide (INH), binding of isoniazid to the active site residues of the enzyme, molecular docking and density functional theory analysis, and modeling using the the molecular mechanics model of the INH-KatG system, detailed overview. Seven amino acid residues directly interact with INH: Arg104, Asp137, His108, Ile228, Trp107, Tyr229, and Val230 Mycobacterium tuberculosis ?
-
 ?
isoniazid + H2O2 pro-drug activation Mycobacterium tuberculosis H37Rv ?
-
 ?
isoniazid + H2O2 i.e. isonicotinylhydrazide (INH), binding of isoniazid to the active site residues of the enzyme, molecular docking and density functional theory analysis, and modeling using the the molecular mechanics model of the INH-KatG system, detailed overview. Seven amino acid residues directly interact with INH: Arg104, Asp137, His108, Ile228, Trp107, Tyr229, and Val230 Mycobacterium tuberculosis H37Rv ?
-
 ?
isoniazid + H2O2 pro-drug activation Mycobacterium tuberculosis ATCC 25618 ?
-
 ?
isoniazid + H2O2 i.e. isonicotinylhydrazide (INH), binding of isoniazid to the active site residues of the enzyme, molecular docking and density functional theory analysis, and modeling using the the molecular mechanics model of the INH-KatG system, detailed overview. Seven amino acid residues directly interact with INH: Arg104, Asp137, His108, Ile228, Trp107, Tyr229, and Val230 Mycobacterium tuberculosis ATCC 25618 ?
-
 ?

Synonyms

Synonyms Comment Organism
catalase peroxidase
-
 Mycobacterium tuberculosis
KatG
-
 Mycobacterium tuberculosis
Rv1908c
-
 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
heme
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
physiological function isoniazid (INH) causes the exclusive lethal action to Mycobacterium tuberculosis cells because of the pathogen's own catalase peroxidase (katG) enzyme that converts INH. Catalase peroxidase (katG) binds and catalyzes the conversion of INH to a very reactive radical. The activated INH, the radical, then reacts with nicotinamide adenine dinucleotide (NAD), a substrate of the enoyl acyl carrier protein reductase (InhA) of the pathogen to form an INH-NAD adduct which irreversibly binds to the InhA. InhA is a crucial protein to produce an important cell wall component of the Mycobacterium tuberculosis cells, thus its inhibition through the irreversible binding of the INH-NAD adduct proves fatal to the pathogen Mycobacterium tuberculosis