EC Number |
Protein Variants |
Reference |
---|
1.1.1.25 | A213L |
site-directed mutagenesis, analysis of substrate and cofactor binding compared to wild-type enzyme |
761595 |
1.1.1.25 | A243G |
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme |
762311 |
1.1.1.25 | D103X |
site-directed mutagenesis of paralogue HI0607, inactive mutant |
669328 |
1.1.1.25 | D105A |
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid |
698320 |
1.1.1.25 | D105N |
site-directed mutagenesis, analysis of substrate and cofactor binding compared to wild-type enzyme |
761595 |
1.1.1.25 | D105N |
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid |
698320 |
1.1.1.25 | D195E |
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme |
762311 |
1.1.1.25 | D423A |
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, inactive mutant |
667700 |
1.1.1.25 | D423N |
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme |
667700 |
1.1.1.25 | G338S/G381T/D483N/L484R/D485T |
site-directed mutagenesis, mutant MTCsDQD/SDHb has a similar reduction activity of 3-DHS and had six times higher oxidation activity of SA than wild-type isozyme CsDQD/SDHb, suggesting that the mutation of residues Ser338 and NRT to Gly and DI/LD in the SDH unit is the reason for the low activity of CsDQD/SDHb, respectively |
761171 |