EC Number |
Protein Variants |
Reference |
---|
5.4.3.8 | K272A |
mutant enzyme Lys272Ala is inactive |
3421 |
5.4.3.8 | more |
gabaculine-resistant mutant enzyme with a 3 times lower catalytic efficiency and impaired prototropic rearrangement and transaldimination |
3430 |
5.4.3.8 | L265E |
mutant Lys265Arg has 2% of the enzymatic activity compared to the wild-type enzyme, the dimeric structure is not influenced, activity is stimulated by addition of exogenous amines such as ethanolamine and methylamine |
3432 |
5.4.3.8 | M248I |
the M248I point mutation confers about 100fold increased gabaculine resistance to GSAM |
703619 |
5.4.3.8 | K286A |
site-directed mutagenesis |
-, 747005 |
5.4.3.8 | more |
improved biological production of 5-aminolevulinate in Corynebacterium glutamicum is achieved by overexpressing the glutamate-initiated C5 pathway. Copies of the glutamyl t-RNA reductase HemA from several bacteria (Corynebacterium glutamicum, Escherichia coli, Bacillus subtilis, Salmonella typhimurium, and Klebsiella pneumoniae) are mutated by site-directed mutagenesis of which a HemA version from Salmonella typhimurium exhibits the highest 5-aminolevulinate production. Cultivation of the HemA-expressing strain produces approximately 204 mg/l of 5-aminolevulinate, while co-expression with HemL (glutamate-1-semialdehyde amino-transferase) increases 5-aminolevulinate concentration to 457 mg/L, representing 11.6fold and 25.9fold increases over the control strain (17 mg/l of 5-aminolevulinate). 5-Aminolevulinate overproduction can also be increased by reducing the formation of heme, which has been shown to have inhibitory effects on HemA activity. Method evaluation and optimization, overview |
-, 747678 |