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	additional information	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