Articles with "enoyl thioester" as a keyword



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A conserved threonine prevents self-intoxication of enoyl-thioester reductases.

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Published in 2017 at "Nature chemical biology"

DOI: 10.1038/nchembio.2375

Abstract: Enzymes are highly specific biocatalysts, yet they can promote unwanted side reactions. Here we investigated the factors that direct catalysis in the enoyl-thioester reductase Etr1p. We show that a single conserved threonine is essential to… read more here.

Keywords: enoyl thioester; conserved threonine; side reactions;