ArticleChemistry (Weinheim an der Bergstrasse, Germany)2021
A Photoclick-Based High-Throughput Screening for the Directed Evolution of Decarboxylase OleT.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Empowering Precision C-H Functionalization: Advances in Peroxygenase Engineering.Angewandte Chemie (International ed. in English) · 2026Review
- Enzyme engineering for functional lipids synthesis: recent advance and perspective.Bioresources and bioprocessing · 2024Review
- Fluorogenic Reactions in Chemical Biology: Seeing Chemistry in Cells.Chemical & biomedical imaging · 2023Review
- A Unique P450 Peroxygenase System Facilitated by a Dual-Functional Small Molecule: Concept, Application, and Perspective.Antioxidants (Basel, Switzerland) · 2022Review
- Toolbox for the structure-guided evolution of ferulic acid decarboxylase (FDC).Scientific reports · 2022Article
- A Photoclick-Based High-Throughput Screening for the Directed Evolution of Decarboxylase OleT.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Enzymatic oxidative decarboxylation is an up-and-coming reaction yet lacking efficient screening methods for the directed evolution of decarboxylases. Here, we describe a simple photoclick assay for the detection of decarboxylation products and its application in a proof-of-principle directed evolution study on the decarboxylase OleT. The assay was compatible with two frequently used OleT operation modes (directly using hydrogen peroxide as the enzyme's co-substrate or using a reductase partner) and the screening of saturation mutagenesis libraries identified two enzyme variants shifting the enzyme's substrate preference from long chain fatty acids toward styrene derivatives. Overall, this photoclick assay holds promise to speed-up the directed evolution of OleT and other decarboxylases.
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