EC Number   |
|---|
    1.17.1.9 | a series of bifunctional enzyme complexes are produced by fusing leucine dehydrogenase and formate dehydrogenase with different peptide linkers, which are expressed in Escherichia coli, purified, and exhibit varied parental enzyme activities and varied L-tert leucine catalytic efficiency. The enzymatic reaction system for L-tert-leucine production and cofactor regeneration with suitable peptide linker is potentially more excellent than free enzymes with lower labor-cost on purification, better thermal stability and higher catalytic efficiency compared with the free coupling of parental enzymes |
| 1.17.1.9 | a tagged, functional enzyme can be continuously secreted by Pichia pastoris. The protein can be easily separated from the growth media using Ni-NTA resin and the activity of the enzyme remains constant even after prolonged growth at 29°C |
| 1.17.1.9 | expressed in Arabidopsis thaliana and Nicotiana tabacum |
| 1.17.1.9 | expressed in Enterobacter aerogenes strain IAM118 |
| 1.17.1.9 | expressed in Enterobacter aerogenes strain IAM1183 |
| 1.17.1.9 | expressed in Escherichia coli |
| 1.17.1.9 | expressed in Escherichia coli BL21 (DE3) cells |
| 1.17.1.9 | expressed in Escherichia coli BL21 cells |
| 1.17.1.9 | expressed in Escherichia coli BL21(DE3) cells |
| 1.17.1.9 | expressed in Escherichia coli BL21(DE3) cells and Pichia pastoris GS115 cells |
