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 |
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 |
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 |
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+ | - |
? |
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 | - |
- |
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 |
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+ | - |
? |
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 |
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 |
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 |
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 |
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 |