Cover Feature: Biochemical Characterization of β‐Amino Acid Incorporation in Fluvirucin B2 Biosynthesis (ChemBioChem 13/2018)

Jesus F. Barajas (Author), Amin Zargar (Author), Bo Pang (Author), Veronica T. Benites (Author), Jennifer Gin (Author), Edward E. K. Baidoo (Author), Christopher J. Petzold (Author), Nathan J. Hillson (Author), Jay D. Keasling (Author)

Research output: Non-textual form2D/3D (physical products)Research

Abstract

The cover feature picture shows fluvirucin B2 and the origin of the nitrogen atom within its macrolactam core: l‐aspartate. The selection or “loading” of l‐aspartate as the starting building block in fluvirucin B2 production is mediated by a set of core enzymes that process and prime the polyketide synthase. We demonstrate the promiscuity of the loading pathway: its ability to use a range of amino acids and further illustrate its ability to load different β‐amino acids selectively onto a PKS loading platform. More information can be found in the communication by J. D. Keasling et al. on page 1391 in Issue 13, 2018 (DOI: 10.1002/cbic.201800169).
Original languageEnglish
Publication date2018
Edition13
Media of outputOnline
DOIs
Publication statusPublished - 2018

Fingerprint

Dive into the research topics of 'Cover Feature: Biochemical Characterization of β‐Amino Acid Incorporation in Fluvirucin B2 Biosynthesis (ChemBioChem 13/2018)'. Together they form a unique fingerprint.

Cite this