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Literature summary for 1.3.1.118 extracted from

  • Nguyen, M.; Quemard, A.; Broussy, S.; Bernadou, J.; Meunier, B.
    Mn(III) pyrophosphate as an efficient tool for studying the mode of action of isoniazid on the InhA protein of Mycobacterium tuberculosis (2002), Antimicrob. Agents Chemother., 46, 2137-2144 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
pharmacology structural investigations of reactive isoniazid species in order to promote the design of new inhibitors of InhA as potential antituberculous drugs Mycobacterium tuberculosis

Cloned(Commentary)

Cloned (Comment) Organism
overexpressed in Escherichia coli Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
isoniazid-coenzyme adduct inhibition by several types of isoniazid-coenzyme adducts coexisting in solution is discussed in relation with the structure of the coenzyme, the stereochemistry of the adducts, and their existence as both open and cyclic forms Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Synonyms

Synonyms Comment Organism
enoyl-acyl carrier protein reductase
-
Mycobacterium tuberculosis
InhA Protein
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Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NADH natural cofactor Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism key enzyme involved in the biosynthesis of long-chain fatty acids and of mycolic acids, specific components of the mycobacterial cell wall Mycobacterium tuberculosis