Details
| Original language | English |
|---|---|
| Pages (from-to) | 11423-11429 |
| Number of pages | 7 |
| Journal | Angewandte Chemie - International Edition |
| Volume | 60 |
| Issue number | 20 |
| Early online date | 4 Mar 2021 |
| Publication status | Published - 10 May 2021 |
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.
Keywords
- iterative polyketide synthase, ketoreductase, mellein, terrein, trans-acting domain
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Chemistry(all)
- General Chemistry
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In: Angewandte Chemie - International Edition, Vol. 60, No. 20, 10.05.2021, p. 11423-11429.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Biosynthesis of 6-Hydroxymellein Requires a Collaborating Polyketide Synthase-like Enzyme
AU - Kahlert, Lukas
AU - Villanueva, Miranda
AU - Cox, Russell J.
AU - Skellam, Elizabeth J.
N1 - Funding Information: Matthias Brock is thanked for the gift of Aspergillus terreus SBUG844. Philipp Budde, Anusha Din, Daniel Saad, and Frank Kulow are thanked for technical assistance. L.K. was funded by DFG (CO 1328/5-1), M.V. was funded by the American Chemical Society visiting scholars programme (2016). DFG is thanked for the provision of LCMS (DFG, INST 187/621-1,) and NMR (INST 187/686-1) instrumentation. Open access funding enabled and organized by Projekt DEAL.
PY - 2021/5/10
Y1 - 2021/5/10
N2 - 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.
AB - 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.
KW - iterative polyketide synthase
KW - ketoreductase
KW - mellein
KW - terrein
KW - trans-acting domain
UR - http://www.scopus.com/inward/record.url?scp=85104062875&partnerID=8YFLogxK
U2 - 10.1002/anie.202100969
DO - 10.1002/anie.202100969
M3 - Article
VL - 60
SP - 11423
EP - 11429
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
SN - 1433-7851
IS - 20
ER -