Stereoselective synthesis of l-tert-leucine by a newly cloned leucine dehydrogenase from Exiguobacterium sibiricum

@inproceedings{Li2014StereoselectiveSO,
  title={Stereoselective synthesis of l-tert-leucine by a newly cloned leucine dehydrogenase from Exiguobacterium sibiricum},
  author={Jing Li and Jiang Qiong Pan and Jie Zhang and Jian-he Xu},
  year={2014}
}
Abstract A leucine dehydrogenase from Exiguobacterium sibiricum ( Es LeuDH) was discovered by genome mining approach. The Es LeuDH was overexpressed in Escherichia coli BL21, purified to homogeneity and characterized. This enzyme showed good thermostability with a half-life of 3.1 h at 60 °C. Furthermore, Es LeuDH has a broad spectrum of substrate specificity, showing activities toward many aliphatic α -keto acids and L -amino acids, in addition to some aryl α -keto acids and aryl α -amino… CONTINUE READING

Similar Papers

Topics from this paper.

Citations

Publications citing this paper.