Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 143, Issue 1, Pages 80-84Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.0c11226
Keywords
-
Categories
Funding
- NIH [1R35GM118056, GM124480]
Ask authors/readers for more resources
Medium-ring lactones are synthetically challenging due to unfavorable energetics in cyclization. The enzyme DcsB from the decarestrictine C1 biosynthetic pathway has been discovered to efficiently catalyze medium-ring lactonizations, showing broad substrate promiscuity. Insights into the molecular basis of catalysis have been gained through X-ray crystal structure and computational analyses.
Medium-ring lactones are synthetically challenging due to unfavorable energetics involved in cyclization. We have discovered a thioesterase enzyme DcsB, from the decarestrictine C1 (1) biosynthetic pathway, that efficiently performs medium-ring lactonizations. DcsB shows broad substrate promiscuity toward linear substrates that vary in lengths and substituents, and is a potential biocatalyst for lactonization. X-ray crystal structure and computational analyses provide insights into the molecular basis of catalysis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available