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Pure Appl. Chem., 2010, Vol. 82, No. 8, pp. 1585-1597

http://dx.doi.org/10.1351/PAC-CON-09-09-37

Published online 2010-05-13

Trinuclear metal clusters in catalysis by terpenoid synthases

Julie A. Aaron and David W. Christianson*

Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA

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  • Brück Thomas, Kourist Robert, Loll Bernhard: Production of Macrocyclic Sesqui- and Diterpenes in Heterologous Microbial Hosts: A Systems Approach to Harness Nature’s Molecular Diversity. ChemCatChem 2014, n/a. <http://dx.doi.org/10.1002/cctc.201300733>
  • Köksal Mustafa, Potter Kevin, Peters Reuben J., Christianson David W.: 1.55Å-resolution structure of ent-copalyl diphosphate synthase and exploration of general acid function by site-directed mutagenesis. Biochimica et Biophysica Acta (BBA) - General Subjects 2014, 1840, 184. <http://dx.doi.org/10.1016/j.bbagen.2013.09.004>
  • Li Ruiqiong, Chou Wayne K. W., Himmelberger Julie A., Litwin Kevin M., Harris Golda G., Cane David E., Christianson David W.: Reprogramming the Chemodiversity of Terpenoid Cyclization by Remolding the Active Site Contour of epi-Isozizaene Synthase. Biochemistry 2014, 53, 1155. <http://dx.doi.org/10.1021/bi401643u>
  • Li Xu-Wen, Nay Bastien: Transition metal-promoted biomimetic steps in total syntheses. Nat. Prod. Rep. 2014, 31, 533. <http://dx.doi.org/10.1039/c3np70077a>
  • Fesko Kateryna, Gruber-Khadjawi Mandana: Biocatalytic Methods for CC Bond Formation. ChemCatChem 2013, 5, 1248. <http://dx.doi.org/10.1002/cctc.201200709>
  • Chen Mengbin, Al-lami Naeemah, Janvier Marine, D’Antonio Edward L., Faraldos Juan A., Cane David E., Allemann Rudolf K., Christianson David W.: Mechanistic Insights from the Binding of Substrate and Carbocation Intermediate Analogues to Aristolochene Synthase. Biochemistry 2013, 52, 5441. <http://dx.doi.org/10.1021/bi400691v>
  • Köksal Mustafa, Chou Wayne K. W., Cane David E., Christianson David W.: Unexpected Reactivity of 2-Fluorolinalyl Diphosphate in the Active Site of Crystalline 2-Methylisoborneol Synthase. Biochemistry 2013, 52, 5247. <http://dx.doi.org/10.1021/bi400797c>
  • Snyder John Hugh, Qi Xiaoquan: Biosynthesis: Metal matters. Nat Chem Biol 2013, 9, 295. <http://dx.doi.org/10.1038/nchembio.1232>
  • Frick S., Nagel R., Schmidt A., Bodemann R. R., Rahfeld P., Pauls G., Brandt W., Gershenzon J., Boland W., Burse A.: Metal ions control product specificity of isoprenyl diphosphate synthases in the insect terpenoid pathway. Proceedings of the National Academy of Sciences 2013, 110, 4194. <http://dx.doi.org/10.1073/pnas.1221489110>
  • Oldfield Eric, Lin Fu-Yang: Terpen-Biosynthese: Modularitätsregeln. angew chemie 2012, 124, 1150. <http://dx.doi.org/10.1002/ange.201103110>
  • Oldfield Eric, Lin Fu-Yang: Terpene Biosynthesis: Modularity Rules. Angew Chem Int E 2012, 51, 1124. <http://dx.doi.org/10.1002/anie.201103110>
  • Köksal Mustafa, Chou Wayne K. W., Cane David E., Christianson David W.: Structure of 2-Methylisoborneol Synthase from Streptomyces coelicolor and Implications for the Cyclization of a Noncanonical C-Methylated Monoterpenoid Substrate. Biochemistry (Wash ) 2012, 51, 3011. <http://dx.doi.org/10.1021/bi201827a>
  • Köksal Mustafa, Chou Wayne K. W., Cane David E., Christianson David W.: Structure of Geranyl Diphosphate C-Methyltransferase from Streptomyces coelicolor and Implications for the Mechanism of Isoprenoid Modification. Biochemistry (Wash ) 2012, 51, 3003. <http://dx.doi.org/10.1021/bi300109c>
  • Zhang Yonghui, Lin Fu-Yang, Li Kai, Zhu Wei, Liu Yi-Liang, Cao Rong, Pang Ran, Lee Eunhae, Axelson Jordan, Hensler Mary: HIV-1 Integrase Inhibitor-Inspired Antibacterials Targeting Isoprenoid Biosynthesis. ACS Med Chem Lett 2012, 3, 402. <http://dx.doi.org/10.1021/ml300038t>
  • Faraldos Juan A., Gonzalez Veronica, Allemann Rudolf K.: The role of aristolochene synthase in diphosphate activation. Chem Commn 2012, 48, 3230. <http://dx.doi.org/10.1039/c2cc17588f>
  • Han Gye Won, Ko Jaeju, Farr Carol L., Deller Marc C., Xu Qingping, Chiu Hsiu-Ju, Miller Mitchell D., Sefcikova Jana, Somarowthu Srinivas, Beuning Penny J.: Crystal structure of a metal-dependent phosphoesterase (YP_910028.1) from Bifidobacterium adolescentis: Computational prediction and experimental validation of phosphoesterase activity. Proteins 2011, 79, 2146. <http://dx.doi.org/10.1002/prot.23035>
  • Faraldos Juan A., González Verónica, Senske Michael, Allemann Rudolf K.: Templating effects in aristolochene synthase catalysis: elimination versus cyclisation. Biomol Chem 2011, 9, 6920. <http://dx.doi.org/10.1039/c1ob06184d>
  • Köksal Mustafa, Zimmer Ina, Schnitzler Jörg-Peter, Christianson David W.: Structure of Isoprene Synthase Illuminates the Chemical Mechanism of Teragram Atmospheric Carbon Emission. Journal of Molecular Biology 2010, 402, 363. <http://dx.doi.org/10.1016/j.jmb.2010.07.009>