Literature summary for 1.3.1.10 extracted from

Khan, R.; Zeb, A.; Roy, N.; Magar, R.; Kim, H.; Lee, K.; Lee, S.
Biochemical and structural basis of triclosan resistance in a novel enoyl-acyl carrier protein reductase (2018), Antimicrob. Agents Chemother., 62, e00648 .

Search for more literature for 1.3.1.10

Protein Variants

Protein Variants	Comment	Organism
additional information	deletion of the loop from Tyr96 to Val101 via site-directed mutagenesis results in the loss of triclosan resistance. The mutant FabL2 retains its enoyl-acyl carrier protein reductase activity	uncultured bacterium pBF1

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	triclosan is not inhibitory due to the presence of an extrapolated six-amino-acid loop specific to FabL2, which prevents the entry of TCL into the active site of FabL2. Elimination of this extrapolated loop via site-directed mutagenesis results in the complete loss of triclosan resistance but not enzyme activity	uncultured bacterium pBF1

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.00963	-	crotonyl-CoA	pH 7.0, 25°C	uncultured bacterium pBF1
0.0276	-	NADPH	pH 7.0, 25°C	uncultured bacterium pBF1

Organism

Organism	UniProt	Comment	Textmining
uncultured bacterium pBF1	A0A1C9U547	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
crotonyl-CoA + NADPH + H+	-	uncultured bacterium pBF1	butanoyl-CoA + NADP+	-	?
additional information	the purified protein exhibits NADPH-dependent enoyl-acyl carrier protein reductases activity but no 7alpha-hydroxysteroid dehydrogenase activity, despite its high homology with 7-AHSDH	uncultured bacterium pBF1	?	-	-

Synonyms

Synonyms	Comment	Organism
Fabl2	-	uncultured bacterium pBF1

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Release 2023.1 (January 2023)