TY - JOUR
T1 - Aryl-aldehyde formation in fungal polyketides
T2 - Discovery and characterization of a distinct biosynthetic mechanism
AU - Wang, Meng
AU - Beissner, Mirko
AU - Zhao, Huimin
N1 - Funding Information:
This work was supported by the National Academies Keck Futures Initiative on Synthetic Biology and the National Institutes of Health (GM077596). We thank Professor Y. Tang for providing S. cerevisiae strain BJ5464-NpgA.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 2014/2/20
Y1 - 2014/2/20
N2 - Aryl-aldehydes are a common feature in fungal polyketides, which are considered to be exclusively generated by the R domain of nonreducing polyketide synthases (NR-PKSs). However, by cloning and heterologous expression of both cryptic NR-PKS and nonribosomal peptide synthase (NRPS)-like genes from Aspergillus terreus in Saccharomyces cerevisiae, we identified a distinct mechanism for aryl-aldehyde formation in which a NRPS-like protein activates and reduces an aryl-acid produced by the accompanying NR-PKS to an aryl-aldehyde. Bioinformatics study indicates that such a mechanism may be widely used throughout the fungi kingdom.
AB - Aryl-aldehydes are a common feature in fungal polyketides, which are considered to be exclusively generated by the R domain of nonreducing polyketide synthases (NR-PKSs). However, by cloning and heterologous expression of both cryptic NR-PKS and nonribosomal peptide synthase (NRPS)-like genes from Aspergillus terreus in Saccharomyces cerevisiae, we identified a distinct mechanism for aryl-aldehyde formation in which a NRPS-like protein activates and reduces an aryl-acid produced by the accompanying NR-PKS to an aryl-aldehyde. Bioinformatics study indicates that such a mechanism may be widely used throughout the fungi kingdom.
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U2 - 10.1016/j.chembiol.2013.12.005
DO - 10.1016/j.chembiol.2013.12.005
M3 - Article
C2 - 24412543
AN - SCOPUS:84894427871
VL - 21
SP - 257
EP - 263
JO - Cell Chemical Biology
JF - Cell Chemical Biology
SN - 2451-9448
IS - 2
ER -