Volume 60, Issue 16 p. 9143
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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)

Dr. Hui Tao

Dr. Hui Tao

Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033 Japan

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Dr. Takahiro Mori

Dr. Takahiro Mori

Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033 Japan

Collaborative Research Institute for Innovative Microbiology, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo, 113-8657 Japan

PRESTO (Japan) Science and Technology Agency, Kawaguchi, Saitama, 332-0012 Japan

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Xingxing Wei

Xingxing Wei

Department of Chemistry, City University of Hong Kong, Tat Chee Avenue, Kowloon, Hong Kong SAR, China

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Dr. Yudai Matsuda

Corresponding Author

Dr. Yudai Matsuda

Department of Chemistry, City University of Hong Kong, Tat Chee Avenue, Kowloon, Hong Kong SAR, China

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Prof. Dr. Ikuro Abe

Corresponding Author

Prof. Dr. Ikuro Abe

Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033 Japan

Collaborative Research Institute for Innovative Microbiology, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo, 113-8657 Japan

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First published: 01 March 2021

Graphical Abstract

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.

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