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

04 December 2020, Version 1
Working Paper
This content is an early or alternative research output and has not been peer-reviewed by Cambridge University Press at the time of posting.

Abstract

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.

Keywords

stereochemistry
biosynthesis
natural product
isostere
enzymology
crystallography

Supplementary materials

Title
Description
Actions
Title
LnmK SI(JRL20201110)
Description
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Now Published

Structures of LnmK, a Bifunctional Acyltransferase/Decarboxylase, with Substrate Analogues Reveal the Basis for Selectivity and Stereospecificity [opens in a new tab]
Lee M. Stunkard, Benjamin J. Kick, Jeremy R. Lohman journal article
Biochemistry , Volume 60, Issue 5
Online publication date: Jan 22, 2021

Version History

Dec 04, 2020 Version 1

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The content is available under CC BY NC ND 4.0 [opens in a new tab]

DOI

10.26434/chemrxiv.13315235.v1
D O I: 10.26434/chemrxiv.13315235.v1 [opens in a new tab]

Author’s competing interest statement

The authors declare no competing financial interests

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