Biomimetic catalytic transformation of toxic α-oxoaldehydes to high-value chiral α-hydroxythioesters using artificial glyoxalase I
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Link
http://www.nature.com/articles/ncomms14877.pdf
Reference41 articles.
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2. Thornalley, P. J. Glyoxalase I – structure, function and a critical role in the enzymatic defence against glycation. Biochem. Soc. Transact. 31, 1343–1348 (2003).
3. Mohr, J. T., Hong, A. Y. & Stoltz, B. M. Enantioselective protonation. Nat. Chem. 1, 359–369 (2009).
4. Himo, F. & Siegbahn, P. E. M. Catalytic mechanism of glyoxalase I: a theoretical study. J. Am. Chem. Soc. 123, 10280–10289 (2001).
5. Cameron, A. D. et al. Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue. Biochemistry 38, 13480–13490 (1999).
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