By combining structure-based computational predictions and a thorough structural analysis, a highly thermostable enzyme, alcohol dehydrogenase, has been engineered.

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

By partitioning promiscuous enzymes across multiple Golgi compartments, eukaryotic cells can tightly control the synthesis of complex sugar oligomers.

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.

Comparative -omic analyses of five knockout mouse strains with disrupted mitochondrial DNA expression at different levels provide a high quality resource of altered gene expression patterns that reveal several common secondary patophysiological changes of mitochondrial dysfunction.

By performing ¹⁵N pulse-labeling of mice, the turnover of hundreds of proteins in eye tissues was measured by mass spectrometry that revealed long-lived metabolic enzymes in the lens.

An RNA-mediated mechanism that stabilizes association of the Suv39h enzymes at mouse heterochromatin is defined.

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.