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Complete Reconstitution of a Highly Reducing Iterative Polyketide Synthase
Open accessAbstract
Dissecting Megaenzyme Mechanisms: Filamentous fungi contain a class of multidomain enzymes, the highly-reducing iterative polyketide synthases (HR-IPKSs), which produce important natural products such as the cholesterol-lowering drug lovastatin. To produce their complex products, these megasynthases use multiple catalytic domains repeatedly in different combinations, but mechanistic details remain unclear. Ma et al. (p. 589 ) now report in vitro reconstitution of the complete catalytic function of lovastatin nonaketide synthase (LovB), the megasynthase that works together with a partner enzyme LovC to complete nearly 40 chemical steps required to construct the core of lovastatin. Analyses of the dependency of enzyme function on cofactors and on the partner enzyme elucidate the programming rules for this system.
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Citations
Cited by
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Wang, B., Wang, J., Zhang, W., & Meldrum, D. R. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00344 · Cited by 211
Scalable production of mechanically tunable block polymers from sugar
Xiong, M., Schneiderman, D. K., Bates, F. S., Hillmyer, M. A., & Zhang, K. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404596111 · Cited by 203
Improving Microalgae for Biotechnology—From Genetics to Synthetic Biology
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Metadata
- Authors
- Ma, S. M., Li, J. W.-H., Choi, J. W., Zhou, H., Lee, K. K. M., Moorthie, V. A., Xie, X., Kealey, J. T., Da Silva, N. A., Vederas, J. C., & Tang, Y.
- Venue
- Science
- Published
- 2009-10-23
- Volume
- 326
- Issue
- 5952
- Pages
- 589-592
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2093386502
- Cited by
- 370
- References
- 0
- FWCI
- 14.30
- Type
- journal article
- Language
- en
- Open access
- green
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- Ma, S. M., Li, J. W.-H., Choi, J. W., Zhou, H., Lee, K. K. M., Moorthie, V. A., Xie, X., Kealey, J. T., Da Silva, N. A., Vederas, J. C., & Tang, Y. (2009). Complete Reconstitution of a Highly Reducing Iterative Polyketide Synthase. Science. https://doi.org/10.1126/science.1175602
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