ArticleChembiochem : a European journal of chemical biology2020
An Enzyme Containing the Conserved Domain of Unknown Function DUF62 Acts as a Stereoselective (R
Article in Chembiochem : a European journal of chemical biology, 2020. 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, 8 citations in OpenAlex.
- An Enzymatic Platform for Late-Stage (Radio)isotope Labelling of Oligonucleotides With Methyltransferases.Angewandte Chemie (International ed. in English) · 2026Article
- Bacterial Fluorinase FIA1 and Evolutionarily Related, Lysine-free StDUF62 Show Distinct Diastereoselectivity and Salt Sensitivity.ACS omega · 2025Article
- Biochemical and Structural Studies of the Carminomycin 4-Journal of natural products · 2024Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
Homochirality is a signature of biological systems. The essential and ubiquitous cofactor S-adenosyl-l-methionine (SAM) is synthesized in cells from adenosine triphosphate and l-methionine to yield exclusively the (S,S)-SAM diastereomer. (S,S)-SAM plays a crucial role as the primary methyl donor in transmethylation reactions important to the development and homeostasis of all organisms from bacteria to humans. However, (S,S)-SAM slowly racemizes at the sulfonium center to yield the inactive (R,S)-SAM, which can inhibit methyltransferases. Control of SAM homochirality has been shown to involve homocysteine S-methyltransferases in plants, insects, worms, yeast, and in ∼18 % of bacteria. Herein, we show that a recombinant protein containing a domain of unknown function (DUF62) from the actinomycete bacterium Salinispora tropica functions as a stereoselective (R,S)-SAM hydrolase (adenosine-forming). DUF62 proteins are encoded in the genomes of 21 % of bacteria and 42 % of archaea and potentially represent a novel mechanism to remediate SAM damage.
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Registered trials
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