EC Number   |
Protein Variants |
Reference |
|---|
    6.2.1.14 | H16A |
site-directed mutagenesis, the mutant variant displays only a modest 20% loss in activity relative to the wild-type, reflecting the importance of these other interacting residues in stabilizing CoA binding |
745845 |
| 6.2.1.14 | more |
deletion of the chromosomal bioW through single crossover recombination by integration of recombinant vector pMUTIN4 blocks growth in biotin-free minimal media, growth phenotypes of Bacillus subtilis bioW and bioI mutant strains, overview. Expression of bioW from the Phyper-spank promoter of vector pDR111 inserted at an ectopic site (the amyE locus) restores growth only when promoter activity is induced with IPTG, biotin auxotrophy due to bioW inactivation. Bacillus subtilis strain BI274 has an engineered bio operon driven by a phage SP01 promoter resulting in overproduction of biotin |
-, 745791 |
| 6.2.1.14 | R159A |
site-directed mutagenesis, the activity to hydrolyze adenylates of noncognate substrates is abolished in the mutant. The R159A variant can no longer proofread, but the enzyme still retains ligase activity and can catalyze the formation of pimeloyl-CoA, the mutant demonstrates a notable reduction in turnover, which is in line with the function of the residue in forming the exterior wall of the pimelate-binding cavity |
745845 |
| 6.2.1.14 | R201A |
site-directed mutagenesis, the mutation has little effect on product formation |
745845 |
| 6.2.1.14 | R213A |
site-directed mutagenesis, almost inactive mutant |
-, 745844 |
| 6.2.1.14 | R215A |
site-directed mutagenesis, the mutant demonstrates a substantial reduction in product formation |
745845 |
| 6.2.1.14 | R227E |
site-directed mutagenesis, the mutant shows a turnover with the natural substrate pimelic acid that is reduced by around 25fold to about 4% activity remaining compared to the wild-type |
745844 |
| 6.2.1.14 | R227K |
site-directed mutagenesis, the mutant shows a turnover with the natural substrate pimelic acid that is reduced by around 25fold to about 4% activity remaining compared to the wild-type |
745844 |
| 6.2.1.14 | S182A |
site-directed mutagenesis, the mutant demonstrates a substantial reduction in product formation |
745845 |
| 6.2.1.14 | Y187A |
site-directed mutagenesis, the mutant demonstrates a notable reduction in turnover, which is in line with the function of the residue in forming the exterior wall of the pimelate-binding cavity |
745845 |
