Literature summary for 1.3.1.118 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 .

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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-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

Synonyms	Comment	Organism
2-trans-enoyl-ACP(CoA) reductase	-	Mycobacterium tuberculosis
InhA	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)