Handicap-Recover Evolution Leads to a Chemically Versatile, Nucleophile-Permissive Protease-Reference-Cited by-同舟云学术

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Handicap-Recover Evolution Leads to a Chemically Versatile, Nucleophile-Permissive Protease

Published:2015-07-14 Issue:13 Volume:16 Page:1866-1869
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Shafee Thomas,Gatti-Lafranconi Pietro,Minter Ralph,Hollfelder Florian

Funder

Funded Access

Biotechnology and Biological Sciences Research Council

MedImmune

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Reference56 articles.

1. The Catalytic Site Atlas 2.0: cataloging catalytic sites and residues identified in enzymes

2. Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad

3. Analogous Enzymes: Independent Inventions in Enzyme Evolution

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1. Ultrahigh-Throughput Directed Evolution of a Metal-Free α/β-Hydrolase with a Cys-His-Asp Triad into an Efficient Phosphotriesterase;Journal of the American Chemical Society;2022-12-30

2. Between Protein Fold and Nucleophile Identity: Multiscale Modeling of the TEV Protease Enzyme–Substrate Complex;ACS Omega;2022-10-27

3. Ultrahigh-throughput directed evolution of a metal-free α/β-hydrolase with a Cys-His-Asp triad into an efficient phosphotriesterase;2022-02-14

4. Construction, Investigation and Application of TEV Protease Variants with Improved Oxidative Stability;Journal of Microbiology and Biotechnology;2021-12-28

5. Discovery of an ultraspecific triuret hydrolase (TrtA) establishes the triuret biodegradation pathway;Journal of Biological Chemistry;2021-01

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