Literature DB >> 29141202

Cooperativity and flexibility in enzyme evolution.

Anna Pabis1, Valeria A Risso2, Jose M Sanchez-Ruiz3, Shina Cl Kamerlin4.   

Abstract

Enzymes are flexible catalysts, and there has been substantial discussion about the extent to which this flexibility contributes to their catalytic efficiency. What has been significantly less discussed is the extent to which this flexibility contributes to their evolvability. Despite this, recent years have seen an increasing number of both experimental and computational studies that demonstrate that cooperativity and flexibility play significant roles in enzyme innovation. This review covers key developments in the field that emphasize the importance of enzyme dynamics not just to the evolution of new enzyme function(s), but also as a property that can be harnessed in the design of new artificial enzymes.
Copyright © 2017 The Authors. Published by Elsevier Ltd.. All rights reserved.

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Year:  2017        PMID: 29141202     DOI: 10.1016/j.sbi.2017.10.020

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  24 in total

Review 1.  Tailoring Proteins to Re-Evolve Nature: A Short Review.

Authors:  Angelica Jimenez-Rosales; Miriam V Flores-Merino
Journal:  Mol Biotechnol       Date:  2018-12       Impact factor: 2.695

Review 2.  Conformational dynamics and enzyme evolution.

Authors:  Dušan Petrović; Valeria A Risso; Shina Caroline Lynn Kamerlin; Jose M Sanchez-Ruiz
Journal:  J R Soc Interface       Date:  2018-07       Impact factor: 4.118

Review 3.  Adaptability and specificity: how do proteins balance opposing needs to achieve function?

Authors:  Bentley Wingert; James Krieger; Hongchun Li; Ivet Bahar
Journal:  Curr Opin Struct Biol       Date:  2020-10-11       Impact factor: 6.809

4.  Microsecond dynamics in proteins by two-dimensional ESR: Predictions.

Authors:  Pranav Gupta; Zhichun Liang; Jack H Freed
Journal:  J Chem Phys       Date:  2020-06-07       Impact factor: 3.488

5.  Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator.

Authors:  Daiana A Capdevila; Fidel Huerta; Katherine A Edmonds; My Tra Le; Hongwei Wu; David P Giedroc
Journal:  Elife       Date:  2018-10-17       Impact factor: 8.140

6.  Structural and biochemical consequences of pyridoxine-dependent epilepsy mutations that target the aldehyde binding site of aldehyde dehydrogenase ALDH7A1.

Authors:  Adrian R Laciak; David A Korasick; Jesse W Wyatt; Kent S Gates; John J Tanner
Journal:  FEBS J       Date:  2019-07-25       Impact factor: 5.542

7.  Two β-Lactamase Variants with Reduced Clavulanic Acid Inhibition Display Different Millisecond Dynamics.

Authors:  Wouter Elings; Aleksandra Chikunova; Danny B van Zanten; Ralphe Drenth; Misbha Ud Din Ahmad; Anneloes J Blok; Monika Timmer; Anastassis Perrakis; Marcellus Ubbink
Journal:  Antimicrob Agents Chemother       Date:  2021-07-16       Impact factor: 5.191

Review 8.  Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.

Authors:  Guillermo Bahr; Lisandro J González; Alejandro J Vila
Journal:  Chem Rev       Date:  2021-06-15       Impact factor: 72.087

9.  Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme Catalysis.

Authors:  Marianne Schulte; Dušan Petrović; Philipp Neudecker; Rudolf Hartmann; Jörg Pietruszka; Sabine Willbold; Dieter Willbold; Vineet Panwalkar
Journal:  ACS Catal       Date:  2018-03-27       Impact factor: 13.084

10.  Protein Flexibility and Stiffness Enable Efficient Enzymatic Catalysis.

Authors:  John P Richard
Journal:  J Am Chem Soc       Date:  2019-02-14       Impact factor: 15.419

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