EC Number   |
|---|
    1.5.3.1 | - |
| 1.5.3.1 | all four subunits |
| 1.5.3.1 | enhancement of soluble expression of codon-optimized enzyme in Escherichia coli via chaperone co-expression |
| 1.5.3.1 | expressed in Escherichia coli BL21 (DE3) in the form of inclusion bodies. Unfolded Bacillus sp. SOX was extracted from an inclusion body and reconstructed with FAD and a group of coenzyme-like compounds. The interactions between the enzyme and various ligands are simulated using molecular docking in the SwissDock service and DS 2.5 program. When the length of the ligand is reduced, the number of H bonds is also reduced. Furthermore, new bonds are formed between the enzyme and the ligands, owing to replacements at the position 7- or 8-sites. Based on the results of structural analysis, phosphoric acid and adenine groups in the natural coenzyme likely play vital roles in maintenance of the enzyme structure. The 7-and 8-site modifications in ligands could facilitate the formation of novel interactions that stabilize the complex. The activities of natural enzyme and refolded FAD-enzyme aree significantly reduced in the presence of organic solvents. However, when the enzyme is refolded with coenzyme-like ligands containing halogen atoms at the position 7- or 8-site, the trend towards reduction is effectively inhibited, and the enzymes exhibit considerably higher relative specificities |
| 1.5.3.1 | expression in Bacillus subtilis |
| 1.5.3.1 | expression in Escherichia coli |
| 1.5.3.1 | expression in Escherichia coli as inclusion body |
| 1.5.3.1 | expression in Escherichia coli strain BL21 |
| 1.5.3.1 | genes TK0116 and TK0117, separate cloning and expression in Eschericia coli strain BL21(DE3) of His-tagged alpha and beta subunits of SOX |
| 1.5.3.1 | integration strategy coupling codon and fermentation optimization is used for efficiently enhancing sarcosine oxidase production in recombinant Escherichia coli |
