X-ray crystallography has been used to observe the synthesis of RNA in the absence of enzymes with atomic resolution.

A unique, widely distributed gut bacterial enzyme selectively metabolizes plant-derived cardiac glycoside drugs.

The stability of metabolic autocatalytic cycles that are widespread in central metabolism limits the affinities of enzymes at flux branch points and explains excess expression of these enzymes.

A catalytically dead paralog activates its cognate enzyme through an allosteric mechanism that combined structural and phylogenomic analysis indicates arose through acquisition of a dimerization domain, suggesting a general model for how complex allostery evolves.

Genetic change among enzyme orthologous with similar phenotypic properties can cause substantial differences in evolutionary response to a new enzyme function in terms of their molecular and fitness outcomes.

An integrated biochemical and evolutionary analysis shows how enzyme specificity evolves after gene loss during genome decay, implicating relaxation of purifying selection as a driving force for functional divergence.

A starvation-induced drop in cytosolic pH promotes assembly of budding yeast glutamine synthetase into enzymatically inactive filaments that function as enzyme storage depots.

Integrative structural analyses of human insulin degradingenzyme (IDE) reveal how IDE selectively degrades peptides that form toxicaggregates, which guides IDE-based therapeutic innovations to treat diabetesand Alzheimer's disease.

Invertebrate TRPM2 channels have stable pores but act as chanzymes that hydrolyze their activating ligand ADP ribose (ADPR), whereas vertebrate TRPM2 channels are catalytically dead but undergo pore inactivation.