4.3 Review

Amine dehydrogenases: Current status and potential value for chiral amine synthesis

Journal

CHEM CATALYSIS
Volume 2, Issue 6, Pages 1288-1314

Publisher

CELL PRESS
DOI: 10.1016/j.checat.2022.03.018

Keywords

-

Funding

  1. National Key Research and Development Program of China [2021YFC2104100]
  2. National Natural Science Foundation of China [21901058, 21878068, 22078081]
  3. Science and Technology Research Project of Hebei Higher Education [ZD2019045]
  4. Natural Science Foundation of Hebei Province [B2017202056, B2019202216, C2019208174]
  5. Natural Science Foundation of Tianjin City [20JCYBJC00530]
  6. Foundation of Tianjin Key Laboratory of Brine Chemical Engineering and Resource Eco-utilization (Tianjin University of Science and Technology)
  7. Key R&D project of Hebei Province [21372804D, 21372805D]
  8. Science and Technology Program Project of Tianjin [20YDTPJC00260]
  9. ERC [742987]
  10. CoEBio3 Industrial Affiliates

Ask authors/readers for more resources

This review discusses the importance and challenges of AmDHs in chiral-amine synthesis, as well as recent advances and engineering design strategies. By exploring the structures, mechanisms, and mutation studies of AmDHs, as well as the development of optimized reaction systems, guidance and direction are provided for improving the performance and efficiency of AmDHs.
Chiral amines are crucial precursors of various pharmaceutical drugs, fine chemicals, and bioactive molecules. Amine dehydrogenases (AmDHs) have attracted increasing attention for chiral-amine synthesis, with great potentials to overcome the shortcomings of conventional chemical methods. However, the narrow substrate scope and expensive cofactors required can be quite challenging for the AmDHs. A number of attempts have been made to improve AmDHs and their reaction systems. The available AmDHs are mainly obtained by the discovery of the naturalAmDHs and the engineering of amino acid dehydrogenases. In this review, recent advances in the structures, mechanisms, and mutation studies of AmDHs are discussed in detail, facilitating the engineering of AmDHs more efficiently. Besides, various enzyme-coupled and immobilization strategies have been designed to optimize the AmDH- catalyzed reaction systems, not only achieving the cofactor regeneration but also enhancing the productivity. Future research directions for improving the performance and reaction system of AmDHs are evaluated.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.3
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available