Erratum: Pathogen-induced biosynthetic pathways encode defense-related molecules in bread wheat (Proceedings of the National Academy of Sciences of the United States of America (2022) 119 (e2123299119) DOI: 10.1073/pnas.2123299119)

Guy Polturak*, Martin Dippe, Michael J. Stephenson, Rajesh Chandra Misra, Charlotte Owen, Ricardo H. Ramirez-Gonzalez, John F. Haidoulis, Henk Jan Schoonbeek, Laetitia Chartrain, Philippa Borrill, David R. Nelson, James K.M. Brown, Paul Nicholson, Cristobal Uauy, Anne Osbourn*

*Corresponding author for this work

Research output: Contribution to journalComment/debate

Abstract

The authors note that the structure of the product of CYP51H37 (TaHIO), compound 10 (named ellarinacin), has been revised in response to recent identification of a sodium adduct in the compound’s mass spectrum. Ellarinacin was originally assigned an exact mass of 454.34 based on an apparent [Mass + H]+ ion of 455. Identification of a sodium adduct [Mass + Na]+ of 495, demotes this 455 ion to [Mass + H – H2O]+ giving compound 10 (ellarinacin) an exact mass of 472.36. The revised assignment of the 13C & 1H NMR spectra of compound 10 (ellarinacin) consistent with a mass of 472.36 is provided in Fig. 1, along with the original and revised structure. It should also be noted that the reported [Mass + H]+ ion of 497 for the acetylated derivative of ellarinacin (acetyl-ellarinacin - the product of BdACT) is also demoted to [Mass + H – H2O]+ and the respective sodium adduct [Mass + Na]+ is observed at 537. In accordance with the revised structure of ellarinacin, the reaction catalyzed by the CYP51H37 (TaHIO) enzyme is 7,25-hydroxylation, with subsequent formation of a 3,25 ether bridge in ring A. The new figure and its legend appear below.

Original languageEnglish
Article numbere2213011119
JournalProceedings of the National Academy of Sciences of the United States of America
Volume119
Issue number36
DOIs
StatePublished - 6 Sep 2022
Externally publishedYes

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