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Inside Back Cover: One Polyketide Synthase, Two Distinct Products: Trans ‐Acting Enzyme‐Controlled Product Divergence in Calbistrin Biosynthesis (Angew. Chem. Int. Ed. 16/2021)
Author(s) -
Tao Hui,
Mori Takahiro,
Wei Xingxing,
Matsuda Yudai,
Abe Ikuro
Publication year - 2021
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202102305
Subject(s) - polyketide synthase , polyketide , biosynthesis , stereochemistry , acyltransferase , enzyme , polyene , chemistry , atp synthase , natural product , biochemistry
Calbistrin biosynthesis involves an unusual dual‐functional polyketide synthase CalA, which synthesizes both of the two structurally distinct moieties of calbistrins. The product divergence is intriguingly controlled by two trans ‐acting enzymes, a trans ‐acting enoylreductase CalK and a trans ‐acting C‐methyltransferanse CalH, to yield the decalin and polyene portions, respectively. The esterification of the two polyketide parts is catalyzed by the acyltransferase CalD, as reported by Yudai Matsuda, Ikuro Abe, and co‐workers in their Research Article on page 8851.