ArticleChembiochem : a European journal of chemical biology2022
Structure-Guided Modulation of the Catalytic Properties of [2Fe-2S]-Dependent Dehydratases.
Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 13 citations in OpenAlex.
- Unveiling the importance of the C-terminus in the sugar acid dehydratase of the IlvD/EDD superfamily.Applied microbiology and biotechnology · 2024Article
- Structural and Functional Insight into the Mechanism of the Fe-S Cluster-Dependent Dehydratase from Paralcaligenes ureilyticus.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Dihydroxy-Acid Dehydratases From Pathogenic Bacteria: Emerging Drug Targets to Combat Antibiotic Resistance.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Structure-Guided Modulation of the Catalytic Properties of [2Fe-2S]-Dependent Dehydratases.Chembiochem : a European journal of chemical biology · 2022Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
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Abstract
The FeS cluster-dependent dihydroxyacid dehydratases (DHADs) and sugar acid-specific dehydratases (DHTs) from the ilvD/EDD superfamily are key enzymes in the bioproduction of a wide variety of chemicals. We analyzed [2Fe-2S]-dependent dehydratases in silico and in vitro, deduced functionally relevant sequence, structure, and activity relationships within the ilvD/EDD superfamily, and we propose a new classification based on their evolutionary relationships and substrate profiles. In silico simulations and analyses identified several key positions for specificity, which were experimentally investigated with site-directed and saturation mutagenesis. We thus increased the promiscuity of DHAD from Fontimonas thermophila (FtDHAD), showing >10-fold improved activity toward D-gluconate, and shifted the substrate preference of DHT from Paralcaligenes ureilyticus (PuDHT) toward shorter sugar acids (recording a six-fold improved activity toward the non-natural substrate D-glycerate). The successful elucidation of the role of important active site residues of the ilvD/EDD superfamily will further guide developments of this important biocatalyst for industrial applications.
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