NDLI: Molecular basis of methylation and chain-length programming in a fungal iterative highly reducing polyketide synthase† †Electronic supplementary information (ESI) available: Including all experimental, bioinformatic and characterisation details. See DOI: 10.1039/c9sc03173a

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Molecular basis of methylation and chain-length programming in a fungal iterative highly reducing polyketide synthase† †Electronic supplementary information (ESI) available: Including all experimental, bioinformatic and characterisation details. See DOI: 10.1039/c9sc03173a

Content Provider	Semantic Scholar
Author	Yang, Xiao-Long Friedrich, Steffen Piech, Oliver Williams, Katherine Simpson, Thomas J. Cox, Russell J.
Copyright Year	2019
Abstract	Exchange of 32 different sub-fragments of the C-methyltransferase (C-MeT), pseudo-ketoreductase (ΨKR) and ketoreductase (KR) catalytic domains of the tenellin iterative Type I polyketide synthase non ribosomal peptide synthetase (PKS-NRPS) TENS by homologous fragments from the desmethylbassianin (DMBS) and militarinone (MILS) PKS-NRPS led to the creation of chimeric synthetases in which programming fidelity was altered, resulting in the production of mixtures of products with different methylation patterns and chain lengths. Swap of KR domain subfragments with the homologous fragments from the KR of the heptaketide militarinone synthetase resulted in the synthesis of penta, hexa and heptaketides. The results of these and previous experiments are rationalised by considering the existence of competition for acyl-carrier protein (ACP) bound substrates between different catalytic domains of the PKS. In particular, competition between the C-MeT and ketoreductase domains (KR) can account for methylation programming, and competition between the KR and the off-loading NRPS accounts for chain-length selectivity.
Starting Page	8478
Ending Page	8489
Page Count	12
File Format	PDF HTM / HTML
DOI	10.1039/c9sc03173a
Alternate Webpage(s)	http://www.rsc.org/suppdata/c9/sc/c9sc03173a/c9sc03173a1.pdf
Alternate Webpage(s)	https://pubs.rsc.org/en/content/articlepdf/2019/sc/c9sc03173a
PubMed reference number	31803427
Alternate Webpage(s)	https://doi.org/10.1039/c9sc03173a
Journal	Medline
Volume Number	10
Journal	Chemical science
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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