Active Site Plasticity of a Computationally Designed Retro-Aldolase Enzyme-Reference-Cited by-同舟云学术

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Active Site Plasticity of a Computationally Designed Retro-Aldolase Enzyme

Published:2014-03-03 Issue:4 Volume:6 Page:1043-1050
ISSN:1867-3880
Container-title:ChemCatChem
language:en
Short-container-title:ChemCatChem

Author:

Obexer Richard,Studer Sabine,Giger Lars,Pinkas Daniel M.,Grütter Markus G.,Baker David,Hilvert Donald

Funder

Swiss National Science Foundation (SNSF)

ETH Zurich

National Center of Excellence in Research (NCCR)

Defense Advanced Research Projects Agency (DARPA)

Stipendienfonds der Schweizerischen Chemischen Industrie (SSCI)

Publisher

Wiley

Subject

Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Catalysis

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/cctc.201300933/fullpdf

Reference35 articles.

1. Class I aldolases: Substrate specificity, mechanism, inhibitors and structural aspects

2. Organocatalysis of asymmetric aldol reaction. Catalysts and reagents

3. Development of Small Designer Aldolase Enzymes: Catalytic Activity, Folding, and Substrate Specificity

4. A Rationally Designed Aldolase Foldamer

5. A Rationally Designed Aldolase Foldamer

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1. Design and optimization of enzymatic activity in a de novo β‐barrel scaffold;Protein Science;2022-10-26

2. The Unexplored Importance of Fleeting Chiral Intermediates in Enzyme-Catalyzed Reactions;Journal of the American Chemical Society;2021-09-07

3. Designing better enzymes: Insights from directed evolution;Current Opinion in Structural Biology;2021-04

4. An enumerative algorithm for de novo design of proteins with diverse pocket structures;Proceedings of the National Academy of Sciences;2020-08-24

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