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Deconstruction of Iterative Multidomain Polyketide Synthase Function
Open accessAbstract
PksA, which initiates biosynthesis of the environmental carcinogen aflatoxin B1, is one of the multidomain iterative polyketide synthases (IPKSs), a large, poorly understood family of biosynthetic enzymes. We found that dissection of PksA and its reconstitution from selected sets of domains allows the accumulation and characterization of advanced octaketide intermediates bound to the enzyme, permitting the reactions controlled by individual catalytic domains to be identified. A product template (PT) domain unites with the ketosynthase and thioesterase in this IPKS system to assemble precisely seven malonyl-derived building blocks to a hexanoyl starter unit and mediate a specific cyclization cascade. Because the PT domain is common among nonreducing IPKSs, these mechanistic features should prove to be general for IPKS-catalyzed production of aromatic polyketides.
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Schroeckh, V., Scherlach, K., Nützmann, H.-W., Shelest, E., Schmidt-Heck, W., Schuemann, J., Martin, K., Hertweck, C., & Brakhage, A. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901870106 · Cited by 663
Navigating the Fungal Polyketide Chemical Space: From Genes to Molecules
Chooi, Y.-H., & Tang, Y. (2012) · The Journal of Organic Chemistry · doi:10.1021/jo301592k · Cited by 271
Filamentous fungi and mycotoxins in cheese: A review
Hymery, N., Vasseur, V., Coton, M., Mounier, J., Jany, J., Barbier, G., & Coton, E. (2014) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12069 · Cited by 215
Feng, Y., Yang, X., Ji, H., Deng, Z., Lin, S., & Zheng, J. (2022) · Communications Biology · doi:10.1038/s42003-022-03477-8 · Cited by 9
Metadata
- Authors
- Crawford, J. M., Thomas, P. M., Scheerer, J. R., Vagstad, A. L., Kelleher, N. L., & Townsend, C. A.
- Venue
- Science
- Published
- 2008-04-11
- Volume
- 320
- Issue
- 5873
- Pages
- 243-246
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2097288504
- Cited by
- 218
- References
- 0
- FWCI
- 14.28
- Type
- journal article
- Language
- en
- Open access
- green
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