Contribution of Oxyanion Stabilization to Kemp Eliminase Efficiency-Reference-Cited by-同舟云学术

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Contribution of Oxyanion Stabilization to Kemp Eliminase Efficiency

Published:2020-03-19 Issue:8 Volume:10 Page:4460-4464
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Kries Hajo¹^ORCID,Bloch Joël S.¹^ORCID,Bunzel H. Adrian¹^ORCID,Pinkas Daniel M.¹^ORCID,Hilvert Donald¹^ORCID

Affiliation:

1. Laboratory of Organic Chemistry, ETH Zurich, 8093 Zurich, Switzerland

Funder

Eidgen?ssische Technische Hochschule Z?rich

Schweizerischer Nationalfonds zur F?rderung der Wissenschaftlichen Forschung

Studienstiftung des Deutschen Volkes

Stipendienfonds der Schweizer Chemischen Industrie

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.0c00575

Reference33 articles.

1. Subtilisin. Stereochemical mechanism involving transition-state stabilization

2. Site-directed mutagenesis and the role of the oxyanion hole in subtilisin.

3. Evaluating the Catalytic Contribution from the Oxyanion Hole in Ketosteroid Isomerase

4. Fundamental Challenges in Mechanistic Enzymology: Progress toward Understanding the Rate Enhancements of Enzymes

Cited by 18 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Enriching productive mutational paths accelerates enzyme evolution;Nature Chemical Biology;2024-09-11

2. Interplay Between Substrate Polarity and Protein Dynamics in Evolved Kemp Eliminases;ChemCatChem;2024-06-05

3. Epistasis arises from shifting the rate-limiting step during enzyme evolution of a β-lactamase;Nature Catalysis;2024-02-23

4. Comment on: “Computer Simulations Reveal an Entirely Entropic Activation Barrier for the Chemical Step in a Designer Enzyme”;ACS Catalysis;2023-07-28

5. Epistasis Arises from Shifting the Rate-Limiting Step during Enzyme Evolution;2023-06-29

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