Ontology highlight
ABSTRACT:
SUBMITTER: Li B
PROVIDER: S-EPMC4208033 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
Li Bingjuan B Li Yuxia Y Bai Dongmei D Zhang Xin X Yang Huiying H Wang Jie J Liu Gang G Yue Juejie J Ling Yan Y Zhou Dongsheng D Chen Huipeng H
Scientific reports 20141024
Lactobacillus brevis alcohol dehydrogenase (Lb-ADH) catalyzes reduction of prochiral carbonyl compounds to chiral alcohol and meanwhile consumes its cofactor NADH into NAD(+), while the cofactor regeneration can be catalyzed by Candida boidinii formate dehydrogenase (Cb-FDH). This work presents three different Escherichia coli whole-cell biocatalyst systems expressing recombinant ADH/FDH, FDH-LIN1-ADH and FDH-LIN2-ADH, respectively, all of which display very high efficacies of prochiral carbonyl ...[more]