EC Number   |
Protein Variants  |
Reference |
|---|
   1.1.1.358 | D58A |
4.82% activity compared to the wild type enzyme |
724098 |
| 1.1.1.358 | F299A |
19.1% activity compared to the wild type enzyme |
724098 |
| 1.1.1.358 | F300A |
17.8% activity compared to the wild type enzyme |
724098 |
| 1.1.1.358 | H125A |
1.5% activity compared to the wild type enzyme |
724098 |
| 1.1.1.358 | H128A |
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme |
-, 761008 |
| 1.1.1.358 | K264A |
65.7% activity compared to the wild type enzyme |
724098 |
| 1.1.1.358 | K28A |
71.1% activity compared to the wild type enzyme |
724098 |
| 1.1.1.358 | K30A |
55.1% activity compared to the wild type enzyme |
724098 |
| 1.1.1.358 | K88A |
inactive |
724098 |
| 1.1.1.358 | more |
an effective biocatalytic cascade was developed by encapsulating a conjugated polyketone reductase (CPR), glucose dehydrogenase (GDH) and the coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of oxopantolactone (KPL) to synthesize (R)-(-)-pantolactone ((R)-PL). When CduCPR and TgGDH are confined in the sodium alginate (SA)-coated hNFs [CduCPR/TgGDH-Ca3(PO4)2], both of them have excellent reusability and high stability. The SA-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-PL, which exhibits satisfactory stereoselectivity and promotes reusability in repeated batches. The SA coating functioned to competently immobilize the coenzyme NADP+ on the CduCPR/TgGDH-Ca3(PO4)2 hNFs, which maintains the maximum bioactivity to synthesize (R)-PL without exogenous coenzyme addition. Method development, optimization, and evaluation, overview |
-, 762360 |
