Literature summary for 1.3.1.104 extracted from

Kim, K.H.; Ha, B.H.; Kim, S.J.; Hong, S.K.; Hwang, K.Y.; Kim, E.E.
Crystal structures of enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis (2011), J. Mol. Biol., 406, 403-415.

Search for more literature for 1.3.1.104

Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
both free form and complexed with NADP+ and inhibitor triclosan, to 2.2 and 1.8 A resolution, respectively. The substrate-binding region in the apo-FabL structure is found in the open form. In addition, the beta4-alpha5 and beta5-alpha7 regions, which include the catalytic residues as well as the cofactor binding residues, get collapsed into the pocket. These differences result in a tetrameric arrangement totally different from NADH-dependent isoform FabI	Bacillus subtilis

Crystallization (Comment)

Organism

both free form and complexed with NADP+ and inhibitor triclosan, to 2.2 and 1.8 A resolution, respectively. The substrate-binding region in the apo-FabL structure is found in the open form. In addition, the beta4-alpha5 and beta5-alpha7 regions, which include the catalytic residues as well as the cofactor binding residues, get collapsed into the pocket. These differences result in a tetrameric arrangement totally different from NADH-dependent isoform FabI

Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
27100	-	x * 27100, calculated	Bacillus subtilis

Organism

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

Subunits

Subunits	Comment	Organism
?	x * 27100, calculated	Bacillus subtilis

Synonyms

Synonyms	Comment	Organism
FabL	-	Bacillus subtilis

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Release 2023.1 (January 2023)