Literature summary 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.

Application

EC Number	Application	Comment	Organism
1.3.1.9	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

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.3.1.9	Mycobacterium tuberculosis	P9WGR1	-	-
1.3.1.9	Mycobacterium tuberculosis H37Rv	P9WGR1	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
1.3.1.9	enoyl-ACP reductase	-	Mycobacterium tuberculosis
1.3.1.9	InhA	-	Mycobacterium tuberculosis

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.3.1.9	NADH	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)