Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme | Zendy

Kahlert Lukas | Zendy; Villanueva Miranda | Zendy; Cox Russell J. | Zendy; Skellam Elizabeth J. | Zendy

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Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme

Author(s) -

Kahlert Lukas,

Villanueva Miranda,

Cox Russell J.,

Skellam Elizabeth J.

Publication year - 2021

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.202100969

Subject(s) - polyketide synthase , dehydratase , polyketide , biosynthesis , enzyme , biochemistry , chemistry , stereochemistry , computational biology , biology

The polyketide synthase (PKS)‐like protein TerB, consisting of inactive dehydratase, inactive C‐methyltransferase, and functional ketoreductase domains collaborates with the iterative non reducing PKS TerA to produce 6‐hydroxymellein, a key pathway intermediate during the biosynthesis of various fungal natural products. The catalytically inactive dehydratase domain of TerB appears to mediate productive interactions with TerA, demonstrating a new mode of trans‐interaction between iterative PKS components.

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