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Literature summary extracted from

  • Kim, S.J.; Ha, B.H.; Kim, K.H.; Hong, S.K.; Shin, K.J.; Suh, S.W.; Kim, E.E.
    Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus (2010), Biochem. Biophys. Res. Commun., 400, 517-522.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.9 expression in Escherichia coli Bacillus cereus
1.3.1.10 BcFabL from strain 6A5 is expressed in Escherichia coli strain BL21(DE3) as His6-tagged protein Bacillus cereus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.9 apo form and in the ternary complex with NADP+ and an indole naphthyridinone inhibitor, to 3.0 and 2.2 A resolution, respectively. The two structures are almost identical, except for the three stretches that are disordered in the apo form. The apo form exists as a homo-dimer in both crystal and solution, while the ternary complex forms a homo-tetramer. The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation Bacillus cereus
1.3.1.10 FabL in apo form and in the ternary complex with NADP+ and an indole naphthyridinone inhibitor, X-ray diffraction structure determination and analysis Bacillus cereus
1.3.1.10 FabL in apo form and in the ternary complex with NADP+ and inhibitor (E)-N-(1,2-dimethyl-1-H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl) acrylamide, 8 mg/ml protein in 20 mM Tris, pH 8.0, 100 mM NaCl, and 1 mM DTT, is mixed with an equal volume of reservoir solution containing 0.1 M sodium citrate pH 5.6, 8% w/v PEG 10,000 and 0.4 M magnesium acetate, hanging-drop methods, for the ternary BcFabL-NADP+-INH complex, NADP+ and inhibitor are added at the molar ratio of 1:1.5 and 1:5, respectively, equilibration in a stabilizing solution containing 0.1 M sodium citrate, pH 5.6, 8% w/v PEG 10,000, 0.4 M magnesium acetate with 30% v/v ethylene glycol as the cryoprotectant, X-ray diffraction structure determination and analysis at 2.2-3.0 A resolution Bacillus cereus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.10 (E)-N-(1,2-dimethyl-1H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl)acrylamide
-
Bacillus cereus
1.3.1.10 triclosan
-
Bacillus cereus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.10 an acyl-[acyl-carrier protein] + NADP+ Bacillus cereus
-
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
?
1.3.1.10 an acyl-[acyl-carrier protein] + NADP+ Bacillus cereus 6A5
-
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
?
1.3.1.10 an acyl-[acyl-carrier protein] + NADP+ Bacillus cereus DSM 31
-
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.9 Bacillus cereus Q81GI3
-
-
1.3.1.9 Bacillus cereus DSM 31 Q81GI3
-
-
1.3.1.10 Bacillus cereus
-
-
-
1.3.1.10 Bacillus cereus Q81GI3
-
-
1.3.1.10 Bacillus cereus 6A5
-
-
-
1.3.1.10 Bacillus cereus DSM 31 Q81GI3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.10 recombinant His6-tagged BcFabL from Escherichia coli strain BL21(DE3) by nickel affinity and adsorption chromatography and gel filtration Bacillus cereus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.10 an acyl-[acyl-carrier protein] + NADP+
-
Bacillus cereus a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
?
1.3.1.10 an acyl-[acyl-carrier protein] + NADP+ assay method by consumption of beta-nicotinamide adenine dinucleotide phosphate during reduction of trans-2-octenoyl-N-acetylcysteamine as the substrate Bacillus cereus a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
?
1.3.1.10 an acyl-[acyl-carrier protein] + NADP+
-
Bacillus cereus 6A5 a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
?
1.3.1.10 an acyl-[acyl-carrier protein] + NADP+ assay method by consumption of beta-nicotinamide adenine dinucleotide phosphate during reduction of trans-2-octenoyl-N-acetylcysteamine as the substrate Bacillus cereus 6A5 a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
?
1.3.1.10 an acyl-[acyl-carrier protein] + NADP+
-
Bacillus cereus DSM 31 a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
?

Subunits

EC Number Subunits Comment Organism
1.3.1.10 dimer the FabL apo form exists as a homodimer in both crystal and solution Bacillus cereus
1.3.1.10 tetramer the ternary complex of FabL with NADP+ or an indole naphthyridinone inhibitor forms a homotetramer Bacillus cereus
1.3.1.10 tetramer the ternary complex of FabL with NADP+ or the indole naphthyridinone inhibitor (E)-N-(1,2-dimethyl-1-H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl) acrylamide forms a homotetramer Bacillus cereus

Synonyms

EC Number Synonyms Comment Organism
1.3.1.9 FabI
-
Bacillus cereus
1.3.1.10 enoyl-[acyl carrier protein] reductase
-
Bacillus cereus
1.3.1.10 ENR
-
Bacillus cereus
1.3.1.10 FabL
-
Bacillus cereus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.10 NADP+ FabL is NADP+-dependent, the side chain of Lys164 of the Tyr-(Xaa)6-Lys dyad at the active site forms a hydrogen bond with the hydroxyl group of the nicotinamide ribose moiety, binding structure, overview Bacillus cereus
1.3.1.10 NADP+ the side chain of Lys164 of the Tyr-(Xaa)6-Lys dyad at the active site forms a hydrogen bond with the hydroxyl group of the nicotinamide ribose moiety, binding structure, overview Bacillus cereus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.3.1.10 0.00006
-
(E)-N-(1,2-dimethyl-1H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl)acrylamide pH 7.0, 30°C Bacillus cereus

General Information

EC Number General Information Comment Organism
1.3.1.10 metabolism ENR is an essential enzyme in type II fatty-acid synthesis that catalyzes the last step in each elongation cycle Bacillus cereus