EC Number   |
Protein Variants |
Reference |
|---|
   1.2.1.84 | G101A |
the activity of the variant is decreased by 62.2% after incubation with short-chain lauroyl-CoA at pH 8.0 and 30°C for 180 min, but 100% activity is lost when using long-chain palmitoyl- and stearoyl-CoAs as the substrate |
763327 |
| 1.2.1.84 | G104A |
the activities of the variant are decreased by 56.1%, 65.9%, and 68.3% toward lauroyl-, palmitoyl-, and stearoyl-CoAs, respectively after 180 min incubation, compared with the wild type enzyme |
763327 |
| 1.2.1.84 | K156A |
the mutant shows increased activity compared to the wild type enzyme |
763058 |
| 1.2.1.84 | K527A |
inactive |
763058 |
| 1.2.1.84 | more |
construction of enzyme-defective mutants, phenotypes, overview |
742343 |
| 1.2.1.84 | more |
de novo fatty alcohol production in Escherichia coli strain AL338 containing plasmidpAL144 or strain AL306, with fadD gene, encoding fatty acyl-CoA synthase, and maqu_2507 gene, method optimization. Biosynthetic pathways of fatty alcohols in genetically engineered Escherichia coli, overview. The amount of fatty alcohols in AL339 is significantly increased to 218.2 mg/l, 9fold higher than that of the control strain AL338. The percentage of medium chain fatty alcohols (12:1, 12:0, 14:1, 14:0, and 16:1) in total fatty alcohols are dramatically increased, especially the C12 and C14 fatty alcohols, accounting for 89% of total fatty alcohols. At the same time, the percentage of C16 and C18 fatty alcohols drops drastically from more than 60% to about 9% and from more than 15% to less than 2%, respectively |
741734 |
| 1.2.1.84 | more |
de novo fatty alcohol production in Escherichia coli strain AL379 containing plasmidpAL144 or in strain AL307, with fadD gene, encoding fatty acyl-CoA synthase, and maqu_2220 gene, method optimization. Biosynthetic pathways of fatty alcohols in genetically engineered Escherichia coli, composition and amounts of fatty alcohols, overview |
741734 |
| 1.2.1.84 | more |
Far1, but not Far2, is preferentially degraded in response to the cellular level of plasmalogens. Experiments in which regions of Far1 or Far2 are replaced with the corresponding region of the other protein show that the region flanking the transmembrane domain of Far1 is required for plasmalogen-dependent modulation of Far1 stability. Expression of Far1 increased plasmalogen synthesis in wild-type Chinese hamster ovary (CHO) cells. FLAG-tagged truncated enzyme mutants Far1490 and FLAG-Far1467 are localized in the mitochondrion and cytosol, respectively, localization analysis of tagged enzyme mutants, overview. Mutants FLAG-Far2Far1491/515 and FLAG-Far2Far1466/515 are not degraded, suggesting that the C-terminal 8 amino acids of Far1 do not influence its plasmalogen-dependent degradation. Expression of FLAG-tagged mutant Far1490-Far2 increases plasmalogen synthesis |
742849 |
| 1.2.1.84 | S126D |
the mutant shows reduced activity compared to the wild type enzyme |
763058 |
| 1.2.1.84 | S126D/Y152F/K156A |
the mutant shows increased activity compared to the wild type enzyme |
763058 |
