Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.1.118 extracted from

  • Nguyen, M.; Quemard, A.; Marrakchi, H.; Bernadou, J.; Meunier, B.
    The nonenzymatic activation of isoniazid by MnIII-pyrophosphate in the presence of NADH produces the inhibition of the enoyl-ACP reductase InhA from Mycobacterium tuberculosis (2001), Chemistry, 4, 35-40 .
No PubMed abstract available
Search for more literature for 1.3.1.118

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
isoniazid fast and efficient inhibition of InhA in the presence of NADH and INH using MnIII-pyrophosphate as nonenzymatic reagent. This chemical oxidant might be a useful tool for further mechanistic studies of isoniazid activation in attempts to establish the exact structures of isoniazid reactive species and InhA inhibitor complex(es). Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trans-2-decenoyl-CoA + NADH + H+
-
 Mycobacterium tuberculosis decanoyl-CoA + NAD+
-
 ?

Synonyms

Synonyms Comment Organism
InhA
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism the enzyme is involved on the biosynthetic pathway for mycolic acids Mycobacterium tuberculosis