TY - JOUR
T1 - Erratum
T2 - 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)
AU - Polturak, Guy
AU - Dippe, Martin
AU - Stephenson, Michael J.
AU - Misra, Rajesh Chandra
AU - Owen, Charlotte
AU - Ramirez-Gonzalez, Ricardo H.
AU - Haidoulis, John F.
AU - Schoonbeek, Henk Jan
AU - Chartrain, Laetitia
AU - Borrill, Philippa
AU - Nelson, David R.
AU - Brown, James K.M.
AU - Nicholson, Paul
AU - Uauy, Cristobal
AU - Osbourn, Anne
N1 - Publisher Copyright:
© 2022 National Academy of Sciences. All rights reserved.
PY - 2022/9/6
Y1 - 2022/9/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85137096839&partnerID=8YFLogxK
U2 - 10.1073/pnas.2213011119
DO - 10.1073/pnas.2213011119
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C2 - 36048911
AN - SCOPUS:85137096839
SN - 0027-8424
VL - 119
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 36
M1 - e2213011119
ER -