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Structures of LnmK a Bifunctional Acyltransferase/Decarboxylase with Substrate Analogs Reveals Basis for Selectivity and Stereospecificity

preprint
submitted on 01.12.2020, 20:09 and posted on 04.12.2020, 11:27 by Lee M Stunkard, Benjamin J. Kick, Jeremy Lohman
We solved crystal structures of LnmK, which that carries out both acyltransfer and decarboxylation in polyketide synthase pathways. Our structures have substrate analogs bound that reveal interactions that likely occur with the substrate and allow modelling of conformational changes and intermediate states.

History

Email Address of Submitting Author

jlohman@purdue.edu

Institution

Purdue University

Country

United States

ORCID For Submitting Author

0000-0001-8199-2344

Declaration of Conflict of Interest

The authors declare no competing financial interests

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