Highly Enantioselective Mutant Carbonyl Reductases Created via Structure-Based Site-Saturation Mutagenesis-Reference-Cited by-同舟云学术

Highly Enantioselective Mutant Carbonyl Reductases Created via Structure-Based Site-Saturation Mutagenesis

Published:2010-10-22 Issue:22 Volume:75 Page:7559-7564
ISSN:0022-3263
Container-title:The Journal of Organic Chemistry
language:en
Short-container-title:J. Org. Chem.

Author:

Li Hongmei¹,Yang Yan¹,Zhu Dunming²¹,Hua Ling¹³,Kantardjieff Katherine⁴

Affiliation:

1. Department of Chemistry, Southern Methodist University, Dallas, Texas 75275, United States

2. State Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China

3. China Research Center, Genencor, A Danisco Division, Shanghai 200335, China

4. Department of Chemistry, California State Polytechnic University, Pomona, California 91768, United States

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jo101541n

Reference31 articles.

1. Advances in the Enzymatic Reduction of Ketones

2. Biocatalytic Reductions: From Lab Curiosity to “First Choice”

3. Recent advances in the biocatalytic reduction of ketones and oxidation of sec -alcohols

4. Practical chiral alcohol manufacture using ketoreductases

5. Combined Ruthenium(II) and Lipase Catalysis for Efficient Dynamic Kinetic Resolution of Secondary Alcohols. Insight into the Racemization Mechanism

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