Substituting the catalytic proline of 4-oxalocrotonate tautomerase with non-canonical analogues reveals a finely tuned catalytic system
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-019-39484-9.pdf
Reference35 articles.
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2. Geertsema, E. M. et al. Biocatalytic Michael-type additions of acetaldehyde to nitroolefins with the proline-based enzyme 4-oxalocrotonate tautomerase yielding enantioenriched γ-nitroaldehydes. Chem. Eur. J. 19, 14407–14410 (2013).
3. Miao, Y., Geertsema, E. M., Tepper, P. G., Zandvoort, E. & Poelarends, G. J. Promiscuous catalysis of asymmetric Michael-type additions of linear aldehydes to β-nitrostyrene by the proline-based enzyme 4-oxalocrotonate tautomerase. ChemBioChem 14, 191–194 (2013).
4. Hamelberg, D., Shen, T. & McCammon, J. A. A proposed signaling motif for nuclear import in mRNA processing via the formation of arginine claw. Proc. Natl. Acad. Sci. USA 104, 14947–14951 (2007).
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