An evolutionary biochemist's perspective on promiscuity

SD Copley - Trends in biochemical sciences, 2015 - cell.com
Evolutionary biochemists define enzyme promiscuity as the ability to catalyze secondary
reactions that are physiologically irrelevant, either because they are too inefficient to affect …

Evolution of efficient pathways for degradation of anthropogenic chemicals

SD Copley - Nature chemical biology, 2009 - nature.com
Anthropogenic compounds used as pesticides, solvents and explosives often persist in the
environment and can cause toxicity to humans and wildlife. The persistence of …

Biosynthesis of menaquinone (vitamin K2) and ubiquinone (coenzyme Q): a perspective on enzymatic mechanisms

R Meganathan - Vitamins & Hormones, 2001 - Elsevier
The benzoquinone ubiquinone (coenzyme Q) and the naphthoquinones menaquinone
(vitamin K 2) and demethylmenaquinone are derived from the shikimate pathway, which has …

[HTML][HTML] Enzyme promiscuity: engine of evolutionary innovation

C Pandya, JD Farelli, D Dunaway-Mariano… - Journal of Biological …, 2014 - ASBMB
Catalytic promiscuity and substrate ambiguity are keys to evolvability, which in turn is pivotal
to the successful acquisition of novel biological functions. Action on multiple substrates …

Catalytic Versatility, Stability, and Evolution of the (βα)8-Barrel Enzyme Fold

R Sterner, B Höcker - Chemical Reviews, 2005 - ACS Publications
Natural evolution has yielded enzymes that catalyze virtually all metabolic reactions under
mild conditions with high specificities and enormous rate enhancements. 1 It has been a …

Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity

JA Gerlt, PC Babbitt, I Rayment - Archives of biochemistry and biophysics, 2005 - Elsevier
The members of the mechanistically diverse enolase superfamily catalyze different overall
reactions. Each shares a partial reaction in which an active site base abstracts the α-proton …

[HTML][HTML] Lateral gene transfer and parallel evolution in the history of glutathione biosynthesis genes

SD Copley, JK Dhillon - Genome biology, 2002 - Springer
Background Glutathione is found primarily in eukaryotes and in Gram-negative bacteria. It
has been proposed that eukaryotes acquired the genes for glutathione biosynthesis from the …

[图书][B] From enzyme models to model enzymes

AJ Kirby, F Hollfelder - 2009 - books.google.com
Designing artificial systems with catalytic efficiencies to rival those of natural enzymes is one
of the great challenges facing science today. Our current level of understanding fails the …

Discovering New Enzymes and Metabolic Pathways:  Conversion of Succinate to Propionate by Escherichia coli

T Haller, T Buckel, J Rétey, JA Gerlt - Biochemistry, 2000 - ACS Publications
The Escherichia coli genome encodes seven paralogues of the crotonase (enoyl CoA
hydratase) superfamily. Four of these have unknown or uncertain functions; their existence …

Evolutionary Potential of (β/α)8-Barrels:  Functional Promiscuity Produced by Single Substitutions in the Enolase Superfamily

DMZ Schmidt, EC Mundorff, M Dojka, E Bermudez… - Biochemistry, 2003 - ACS Publications
The members of the mechanistically diverse,(β/α) 8-barrel fold-containing enolase
superfamily evolved from a common progenitor but catalyze different reactions using a …