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O-Methyltransferase Is Shared between the Pentose Phosphate and Shikimate Pathways and Is Essential for Mycosporine-Like Amino Acid Biosynthesis in Anabaena variabilis ATCC 29413

Research output: Contribution to journalArticlepeer-review

Matthew A Pope, Edward Spence, Valentina Seralvo, Ranko Gacesa, Sibylle Heidelberger, Andrew J Weston, Walter C Dunlap, J Malcolm Shick, Paul F Long

Original languageEnglish
Pages (from-to)320-327
Number of pages8
JournalChembiochem : a European journal of chemical biology
Issue number2
Published19 Jan 2015

King's Authors


The parent core structure of mycosporine-like amino acids (MAAs) is 4-deoxygadusol, which, in cyanobacteria, is derived from conversion of the pentose phosphate pathway intermediate sedoheptulose 7-phosphate by the enzymes 2-epi-5-epivaliolone synthase (EVS) and O-methyltransferase (OMT). Yet, deletion of the EVS gene from Anabaena variabilis ATCC 29413 was shown to have little effect on MAA production, thus suggesting that its biosynthesis is not exclusive to the pentose phosphate pathway. Herein, we report how, using pathway-specific inhibitors, we demonstrated unequivocally that MAA biosynthesis occurs also via the shikimate pathway. In addition, complete in-frame gene deletion of the OMT gene from A. variabilis ATCC 29413 reveals that, although biochemically distinct, the pentose phosphate and shikimate pathways are inextricably linked to MAA biosynthesis in this cyanobacterium. Furthermore, proteomic data reveal that the shikimate pathway is the predominate route for UV-induced MAA biosynthesis.

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