Perspective: Defining and quantifying the role of dynamics in enzyme catalysis

A Warshel, RP Bora - The Journal of chemical physics, 2016 - pubs.aip.org
Enzymes control chemical reactions that are key to life processes, and allow them to take
place on the time scale needed for synchronization between the relevant reaction cycles. In …

Conformational dynamics and enzyme evolution

D Petrović, VA Risso, SCL Kamerlin… - Journal of the …, 2018 - royalsocietypublishing.org
Enzymes are dynamic entities, and their dynamic properties are clearly linked to their
biological function. It follows that dynamics ought to play an essential role in enzyme …

Antioxidant properties of HDL

H Soran, JD Schofield, PN Durrington - Frontiers in pharmacology, 2015 - frontiersin.org
High-density lipoprotein (HDL) provides a pathway for the passage of lipid peroxides and
lysophospholipids to the liver via hepatic scavenger receptors. Perhaps more importantly …

The structure and function of paraoxonase-1 and its comparison to paraoxonase-2 and-3

A Taler-Verčič, M Goličnik, A Bavec - Molecules, 2020 - mdpi.com
Serum paraoxonase-1 (PON1) is the most studied member of the group of paraoxonases
(PONs). This enzyme possesses three enzymatic activities: lactonase, arylesterase, and …

Protein engineers turned evolutionists—the quest for the optimal starting point

DL Trudeau, DS Tawfik - Current opinion in biotechnology, 2019 - Elsevier
The advent of laboratory directed evolution yielded a fruitful crosstalk between the
disciplines of molecular evolution and bio-engineering. Here, we outline recent …

Manipulating conformational dynamics to repurpose ancient proteins for modern catalytic functions

JM Gardner, M Biler, VA Risso, JM Sanchez-Ruiz… - ACS …, 2020 - ACS Publications
Conformational flexibility plays a critical role in enzyme function and regulation.
Conformational changes, which can occur on multiple length and time scales, facilitate, for …

Active site hydrophobicity and the convergent evolution of paraoxonase activity in structurally divergent enzymes: the case of serum paraoxonase 1

D Blaha-Nelson, DM Kruger, K Szeler… - Journal of the …, 2017 - ACS Publications
Serum paraoxonase 1 (PON1) is a native lactonase capable of promiscuously hydrolyzing a
broad range of substrates, including organophosphates, esters, and carbonates …

Enzymes, reacting with organophosphorus compounds as detoxifiers: diversity and functions

I Lyagin, E Efremenko - International Journal of Molecular Sciences, 2021 - mdpi.com
Organophosphorus compounds (OPCs) are able to interact with various biological targets in
living organisms, including enzymes. The binding of OPCs to enzymes does not always lead …

Catalytic Redundancies and Conformational Plasticity Drives Selectivity and Promiscuity in Quorum Quenching Lactonases

M Corbella, J Bravo, AO Demkiv, AR Calixto… - JACS Au, 2024 - ACS Publications
Several enzymes from the metallo-β-lactamase-like family of lactonases (MLLs) degrade N-
acyl L-homoserine lactones (AHLs). They play a role in a microbial communication system …

On the origins of enzymes: Phosphate-binding polypeptides mediate phosphoryl transfer to synthesize adenosine triphosphate

P Vyas, S Malitsky, M Itkin… - Journal of the American …, 2023 - ACS Publications
Reactions involving the transfer of a phosphoryl (− PO32–) group are fundamental to cellular
metabolism. These reactions are catalyzed by enzymes, often large and complex, belonging …