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Literature summary extracted from

  • Vasconcelos, I.; Basso, L.; Santos, D.
    Kinetic and equilibrium mechanisms of substrate binding to Mycobacterium tuberculosis enoyl reductase Implications to function-based antitubercular agent design (2010), J. Braz. Chem. Soc., 21, 1503-1508 .
No PubMed abstract available

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.9 Mycobacterium tuberculosis
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-
-
1.3.1.118 Mycobacterium tuberculosis
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-
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Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.9
-
 Mycobacterium tuberculosis
1.3.1.118
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.9 trans-2-dodecenoyl-CoA + NADH + H+ pre-steady state kinetics and equilibrium data of 2-trans-dodecenoyl-CoA substrate binding to InhA. The results indicate both positive homotropic cooperativity upon substrate binding to InhA, and a bimolecular association process followed by a slow isomerization of the enzyme-substrate binary complex Mycobacterium tuberculosis dodecanoyl-CoA + NAD+
-
 ?
1.3.1.118 trans-2-dodecenoyl-CoA + NADH + H+ pre-steady state kinetics and equilibrium data of 2-trans-dodecenoyl-CoA substrate binding to InhA. The results indicate both positive homotropic cooperativity upon substrate binding to InhA, and a bimolecular association process followed by a slow isomerization of the enzyme-substrate binary complex Mycobacterium tuberculosis dodecanoyl-CoA + NAD+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.1.9 2-trans-enoyl-ACP(CoA) reductase
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 Mycobacterium tuberculosis
1.3.1.9 InhA
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 Mycobacterium tuberculosis
1.3.1.118 2-trans-enoyl-ACP(CoA) reductase
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 Mycobacterium tuberculosis
1.3.1.118 InhA
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 Mycobacterium tuberculosis