The evolution of multiple active site configurations in a designed enzyme-Reference-Cited by-同舟云学术

The evolution of multiple active site configurations in a designed enzyme

Published:2018-09-25 Issue:1 Volume:9 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Hong Nan-Sook,Petrović Dušan^ORCID,Lee Richmond,Gryn’ova Ganna,Purg Miha,Saunders Jake,Bauer Paul,Carr Paul D.,Lin Ching-Yeh,Mabbitt Peter D.^ORCID,Zhang William^ORCID,Altamore Timothy,Easton Chris^ORCID,Coote Michelle L.^ORCID,Kamerlin Shina C. L.^ORCID,Jackson Colin J.^ORCID

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/s41467-018-06305-y.pdf

Reference67 articles.

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2. Giger, L. et al. Evolution of a designed retro-aldolase leads to complete active site remodeling. Nat. Chem. Biol. 9, 494–498 (2013).

3. Liu, H. & Warshel, A. Origin of the temperature dependence of isotope effects in enzymatic reactions: the case of dihydrofolate reductase. J. Phys. Chem. B 111, 7852–7861 (2007).

4. Glowacki, D. R., Harvey, J. N. & Mulholland, A. J. Taking Ockham’s razor to enzyme dynamics and catalysis. Nat. Chem. 4, 169–176 (2012).

5. Nagel, Z. D. & Klinman, J. P. A 21st century revisionist’s view at a turning point in enzymology. Nat. Chem. Biol. 5, 543–550 (2009).

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