Literature summary for 1.3.1.104 extracted from

Heath, R.J.; Su, N.; Murphy, C.K.; Rock, C.O.
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis (2000), J. Biol. Chem., 275, 40128-40133.

Search for more literature for 1.3.1.104

Inhibitors

Inhibitors	Comment	Organism	Structure
triclosan	enzyme is reversibly inhibited by triclosan, but does not form a stable ternary complex	Bacillus subtilis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.016	-	NADPH	pH 7.5, 25°C	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P71079	-	-
Bacillus subtilis 168	P71079	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
trans-2-octenoyl-N-acetylcysteamine + NADPH + H+	-	Bacillus subtilis	octanoyl-N-acetylcysteamine + NADP+	-	?
trans-2-octenoyl-N-acetylcysteamine + NADPH + H+	-	Bacillus subtilis 168	octanoyl-N-acetylcysteamine + NADP+	-	?

Synonyms

Synonyms	Comment	Organism
FabL	-	Bacillus subtilis
YgaA	-	Bacillus subtilis

Cofactor

Cofactor	Comment	Organism	Structure
additional information	no cofactor: NADH	Bacillus subtilis
NADPH	enzyme does not exhibit cooperative binding of NADPH	Bacillus subtilis

General Information

General Information	Comment	Organism
physiological function	expression of isoform FabL complements the temperature-sensitive fabI defect in Escherichia coli and confers complete triclosan resistance. Knockouts of the FabL gene in Bacillus subtilis are viable, but double knockouts of isoforms FabI and FabL are not obtained. The ygaA knockout is 250fold more sensitive to triclosan than wild-type	Bacillus subtilis

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Release 2023.1 (January 2023)