Ground-state destabilization by electrostatic repulsion is not a driving force in orotidine-5′-monophosphate decarboxylase catalysis-Reference-Cited by-同舟云学术

Ground-state destabilization by electrostatic repulsion is not a driving force in orotidine-5′-monophosphate decarboxylase catalysis

Published:2022-04-21 Issue:4 Volume:5 Page:332-341
ISSN:2520-1158
Container-title:Nature Catalysis
language:en
Short-container-title:Nat Catal

Author:

Rindfleisch Sören^ORCID,Krull Matthias,Uranga Jon^ORCID,Schmidt Tobias,Rabe von Pappenheim Fabian^ORCID,Kirck Laura Liliana,Balouri Angeliki,Schneider Thomas^ORCID,Chari Ashwin^ORCID,Kluger Ronald,Bourenkov Gleb^ORCID,Diederichsen Ulf^ORCID,Mata Ricardo A.^ORCID,Tittmann Kai^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Process Chemistry and Technology,Biochemistry,Bioengineering,Catalysis

Link

https://www.nature.com/articles/s41929-022-00771-w.pdf

Reference79 articles.

1. Radzicka, A. & Wolfenden, R. A proficient enzyme. Science 267, 90–93 (1995).

2. Lee, J. K. & Houk, K. N. A proficient enzyme revisited: the predicted mechanism for orotidine monophosphate decarboxylase. Science 276, 942–945 (1997).

3. Miller, B. G. & Wolfenden, R. Catalytic proficiency: the unusual case of OMP decarboxylase. Annu. Rev. Biochem. 71, 847–885 (2002).

4. Richard, J. P., Amyes, T. L. & Reyes, A. C. Orotidine 5′-monophosphate decarboxylase: probing the limits of the possible for enzyme catalysis. Acc. Chem. Res. 51, 960–969 (2018).

5. Wu, N., Mo, Y., Gao, J. & Pai, E. F. Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase. Proc. Natl Acad. Sci. USA 97, 2017–2022 (2000).

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