Literature summary for 1.3.1.9 extracted from

Protasevich, II; Brouillette, C.G.; Snow, M.E.; Dunham, S.; Rubin, J.R.; Gogliotti, R.; Siegel, K.
Role of inhibitor aliphatic chain in the thermodynamics of inhibitor binding to Escherichia coli enoyl-ACP reductase and the Phe203Leu mutant: a proposed mechanism for drug resistance (2004), Biochemistry, 43, 13380-13389.

Search for more literature for 1.3.1.9

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
F203L	drug resistant mutant, probably due to an altered inhibitor-binding mode and a relatively more rigid binding site	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
2-(2-hydroxyphenoxy)phenol	-	Escherichia coli
5-ethyl-2(2-hydroxyphenoxy)phenol	-	Escherichia coli
5-methyl-2(2-hydroxyphenoxy)phenol	-	Escherichia coli
5-propyl-2(2-hydroxyphenoxy)phenol	-	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
28000	-	4 * 28000	Escherichia coli
120100	-	native PAGE	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AEK4	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant FabI	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
trans-2-octenoyl-N-acetylcysteamine + NADH	-	Escherichia coli	octanoyl-N-acetylcysteamine + NAD+	-	?

Subunits

Subunits	Comment	Organism
tetramer	4 * 28000	Escherichia coli

Synonyms

Synonyms	Comment	Organism
FabI	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NADH	-	Escherichia coli

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Release 2023.1 (January 2023)