ArticleThe FEBS journal2023
Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics.
Article in The FEBS journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- ω-Hydroxyacid Dehydrogenases From Clostridium viride: Iron-Containing Biocatalysts With Biotechnological Potential.Chembiochem : a European journal of chemical biology · 2026Article
- From plastic waste to bioprocesses: Using ethylene glycol from polyethylene terephthalate biodegradation to fuelMetabolic engineering communications · 2024Article
- Novel aspects of ethylene glycol catabolism.Applied microbiology and biotechnology · 2024Review
- Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A group-III iron containing 1,2-propanediol oxidoreductase, FucO, (also known as lactaldehyde reductase) from Escherichia coli was examined regarding its structure-dynamics-function relationships in the catalysis of the NADH-dependent reduction of (2S)-lactaldehyde. Crystal structures of FucO variants in the presence or absence of cofactors have been determined, illustrating large domain movements between the apo and holo enzyme structures. Different structures of FucO variants co-crystallized with NAD
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