Quantification of N-acetylcysteamine activated methylmalonate incorporation into polyketide biosynthesis

Scholarly Works

• Saeed, A. U.; Rahman, M. U.; Chen, H.-F.; Zheng, J. Structural Insight of KSIII (β-Ketoacyl-ACP Synthase)-like Acyltransferase ChlB3 in the Biosynthesis of Chlorothricin. Molecules (Basel, Switzerland) 2022, 27, 6405. doi:10.3390/molecules27196405
• Grote, M.; Schulz, F. Exploring the Promiscuous Enzymatic Activation of Unnatural Polyketide Extender Units in Vitro and in Vivo for Monensin Biosynthesis. Chembiochem : a European journal of chemical biology 2019, 20, 1183–1189. doi:10.1002/cbic.201800734
• Möller, D.; Kushnir, S.; Grote, M.; Ismail-Ali, A.; Koopmans, K. R.; Calo, F.; Heinrich, S.; Diehl, B.; Schulz, F. Flexible enzymatic activation of artificial polyketide extender units by Streptomyces cinnamonensis into the monensin biosynthetic pathway. Letters in applied microbiology 2018, 67, 226–234. doi:10.1111/lam.13039
• Musiol-Kroll, E. M.; Wohlleben, W. Acyltransferases as Tools for Polyketide Synthase Engineering. Antibiotics (Basel, Switzerland) 2018, 7, 62. doi:10.3390/antibiotics7030062
• Li, X.; Pei, G.; Liu, L.; Chen, L.; Zhang, W. Metabolomic analysis and lipid accumulation in a glucose tolerant Crypthecodinium cohnii strain obtained by adaptive laboratory evolution. Bioresource technology 2017, 235, 87–95. doi:10.1016/j.biortech.2017.03.049
• Franke, J.; Hertweck, C. Biomimetic Thioesters as Probes for Enzymatic Assembly Lines: Synthesis, Applications, and Challenges. Cell chemical biology 2016, 23, 1179–1192. doi:10.1016/j.chembiol.2016.08.014
• Castelli, K. R.
• Singh, G.; Rani, S.; Arora, A.; Aulakh, D.; Wriedt, M. Thioester-appended organosilatranes: synthetic investigations and application in the modification of magnetic silica surfaces. New Journal of Chemistry 2016, 40, 6200–6213. doi:10.1039/c6nj00011h
• Bravo-Rodriguez, K.; Klopries, S.; Koopmans, K. R.; Sundermann, U.; Yahiaoui, S.; Arens, J.; Kushnir, S.; Schulz, F.; Sanchez-Garcia, E. Substrate Flexibility of a Mutated Acyltransferase Domain and Implications for Polyketide Biosynthesis. Chemistry & biology 2015, 22, 1425–1430. doi:10.1016/j.chembiol.2015.02.008
• Friedrich, S.; Hahn, F. Opportunities for enzyme catalysis in natural product chemistry. Tetrahedron 2015, 71, 1473–1508. doi:10.1016/j.tet.2014.12.026
• Wang, F.; Wang, Y.; Ji, J.; Zhou, Z.; Yu, J.; Zhu, H.; Su, Z.; Zhang, L.; Zheng, J. Structural and Functional Analysis of the Loading Acyltransferase from Avermectin Modular Polyketide Synthase. ACS chemical biology 2015, 10, 1017–1025. doi:10.1021/cb500873k
• Bravo-Rodriguez, K.; Ismail-Ali, A.; Klopries, S.; Kushnir, S.; Ismail, S.; Fansa, E. K.; Wittinghofer, A.; Schulz, F.; Sanchez-Garcia, E. Predicted Incorporation of Non‐native Substrates by a Polyketide Synthase Yields Bioactive Natural Product Derivatives. Chembiochem : a European journal of chemical biology 2014, 15, 1991–1997. doi:10.1002/cbic.201402206
• Dunn, B. J.; Khosla, C. Engineering the acyltransferase substrate specificity of assembly line polyketide synthases. Journal of the Royal Society, Interface 2013, 10, 20130297. doi:10.1098/rsif.2013.0297

Explore citations to this article at