Abstract
NotF from Aspergillus sp. MF297-2 and BrePT from Aspergillus versicolor catalyze a reverse C2-prenylation of brevianamide F in the biosynthetic pathway of brevianamides and notoamides. NotF was reported to use only brevianamide F as substrate while BrePT demonstrated broad substrate promiscuity. With high identity at amino acid level, it is interesting to reinvestigate the catalytic activities of these two prenyltransferases in vitro toward 14 cyclodipeptides. Product identification of the in vitro assays by MS proved that NotF and BrePT share similar catalytic ability and substrate promiscuity.
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Acknowledgements
This work was supported by the National Natural Science Foundation of China (81803409 and 21838001) and the Fundamental Research Funds for the Central Universities (grant numbers buctrc201810, XK1802-8 and PT1909).
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Yang, K., Li, SM., Liu, X. et al. Reinvestigation of the substrate specificity of a reverse prenyltransferase NotF from Aspergillus sp. MF297-2. Arch Microbiol 202, 1419–1424 (2020). https://doi.org/10.1007/s00203-020-01854-7
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DOI: https://doi.org/10.1007/s00203-020-01854-7