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Literature summary for 1.3.1.9 extracted from

  • Stigliani, J.L.; Arnaud, P.; Delaine, T.; Bernardes-Genisson, V.; Meunier, B.; Bernadou, J.
    Binding of the tautomeric forms of isoniazid-NAD adducts to the active site of the Mycobacterium tuberculosis enoyl-ACP reductase (InhA): a theoretical approach (2008), J. Mol. Graph. Model., 27, 536-545.
    View publication on PubMed

Application

Application Comment Organism
medicine the results can be of primary importance in to elucidate the mechanism of action of isoniazid and to better understand the isoniazid-dependent resistances, and they can also prove useful in the design of a new generation of antitubercular drugs Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
isoniazid inhibition involves a covalent attachment of the activated form of the drug to the nicotinamide ring of NADH Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WGR1
-
-
Mycobacterium tuberculosis H37Rv P9WGR1
-
-

Synonyms

Synonyms Comment Organism
enoyl-ACP reductase
-
Mycobacterium tuberculosis
InhA
-
Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NADH
-
Mycobacterium tuberculosis