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PokMT1 from the Polyketomycin Biosynthetic Machinery of Streptomyces diastatochromogenes Tü6028 Belongs to the Emerging Family of C-Methyltransferases That Act on CoA-Activated Aromatic Substrates.
Guo X, Crnovcic I, Chang CY, Luo J, Lohman JR, Papinski M, Bechthold A, Horsman GP, Shen B. Guo X, et al. Among authors: shen b. Biochemistry. 2018 Feb 13;57(6):1003-1011. doi: 10.1021/acs.biochem.7b01219. Epub 2018 Jan 30. Biochemistry. 2018. PMID: 29341603
Structure of the bifunctional acyltransferase/decarboxylase LnmK from the leinamycin biosynthetic pathway revealing novel activity for a double-hot-dog fold.
Lohman JR, Bingman CA, Phillips GN Jr, Shen B. Lohman JR, et al. Among authors: shen b. Biochemistry. 2013 Feb 5;52(5):902-11. doi: 10.1021/bi301652y. Epub 2013 Jan 24. Biochemistry. 2013. PMID: 23320975 Free PMC article.
In vitro biochemical investigation confirmed that LnmK is a bifunctional acyltransferase/decarboxylase (AT/DC) that catalyzes first self-acylation using methylmalonyl-CoA as a substrate and subsequently transacylation of the methylmalonyl group to the phosphopantetheinyl group of …
In vitro biochemical investigation confirmed that LnmK is a bifunctional acyltransferase/decarboxylase (AT/DC) that catalyzes first self-acy …
6,305 results