Literature summary for 1.3.1.9 extracted from

Rafi, S.B.; Cui, G.; Song, K.; Cheng, X.; Tonge, P.J.; Simmerling, C.
Insight through molecular mechanics Poisson-Boltzmann surface area calculations into the binding affinity of triclosan and three analogues for FabI, the E. coli enoyl reductase (2006), J. Med. Chem., 49, 4574-4580.

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Application

Application	Comment	Organism
medicine	antibacterial target	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
2-(2,4-dichlorophenoxy)-5-chlorophenol	triclosan, dissociation constant of the inhibitor from the enzyme-NAD+ product complex: 7.0 pM	Escherichia coli
2-phenoxyphenol	PP, dissociation constant of the inhibitor from the enzyme-NAD+ product complex: 0.5 microM	Escherichia coli
5-chloro-2-phenoxyphenol	CPP, dissociation constant of the inhibitor from the enzyme-NAD+ product complex: 1.1 pM	Escherichia coli
5-fluoro-2-phenoxyphenol	FPP, dissociation constant of the inhibitor from the enzyme-NAD+ product complex: 1.5 nM	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acyl-[acyl-carrier protein] + NAD+	Escherichia coli	-	trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AEK4	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acyl-[acyl-carrier protein] + NAD+	-	Escherichia coli	trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+	-	?

Synonyms

Synonyms	Comment	Organism
enoyl reductase	-	Escherichia coli
enoyl-[acyl-carrier-protein] reductase	-	Escherichia coli
FabI	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NADH	-	Escherichia coli

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Release 2023.1 (January 2023)