Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 50, Pages 22738-22742Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202011357
Keywords
biosynthesis; enoylreductase domain; iterative domain; natural products; polyketide synthases
Categories
Funding
- National Key R&D Program of China [2018YFA0903200]
- Open Funding Project from State Key Laboratory of Microbial Metabolism [MMLKF18-11]
Ask authors/readers for more resources
The colinearity of canonical modular polyketide synthases, which creates a direct link between multienzyme structure and the chemical structure of the biosynthetic end-product, has become a cornerstone of knowledge-based genome mining. Herein, we report genetic and enzymatic evidence for the remarkable role of an enoylreductase in the polyketide synthase for azalomycin F biosynthesis. This internal enoylreductase domain, previously identified as acting only in the second of two chain extension cycles on an initial iterative module, is shown to also catalyze enoylreductionin transwithin the next module. The mechanism for this rare deviation from collinearity appears to involve direct cross-modular interaction of the reductase with the longer acyl chain, rather than back transfer of the substrate into the iterative module, suggesting an additional and surprising plasticity in natural PKS assembly-line 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