Literature summary for 1.3.1.9 extracted from

Bergler, H.; Fuchsbichler, S.; Hoegenauer, G.; Turnowsky, F.
The enoyl-[acyl-carrier-protein] reductase (FabI) of Escherichia coli, which catalyzes a key regulatory step in fatty acid biosynthesis, accepts NADH and NADPH as cofactors and is inhibited by palmitoyl-CoA (1996), Eur. J. Biochem., 242, 689-694.

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Inhibitors

Inhibitors	Comment	Organism	Structure
6-methyl-2-(propane-1-sulfonyl)-4a,7a-dihydro-2H-thieno[3,2-d][1,2,3]diazaborinin-1-ol	diazaborine derviative 2b18, 90% loss of NADH-dependent activity, 50% loss of NADPH-dependent activity at 0.52 mM	Escherichia coli
palmitoyl-CoA	50% inhibition at 0.0054 mM, competitive inhibition	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
33000	-	monomeric form, SDS-PAGE	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	wild type and temperature sensitive mutants	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	specific activities in temperature sensitive mutants	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme uses as well NADH as NADPH	Escherichia coli	?	-	?

Cofactor

Cofactor	Comment	Organism	Structure
NADH	-	Escherichia coli
NADPH	-	Escherichia coli

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.02	-	palmitoyl-CoA	-	Escherichia coli

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Release 2023.1 (January 2023)