By combining structure-based computational predictions and a thorough structural analysis, a highly thermostable enzyme, alcohol dehydrogenase, has been engineered.
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.
The common post-translational modification trans-4-hydroxy-L-proline is reversed by gut microbes with the help of hydroxyproline dehydratase (HypD), an enzyme that performs a radical chemical mechanism.
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.
