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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
Abstract 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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