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.

NMR and biochemical analysis reveal new insights into how the critical protein kinase Akt is regulated by phosphorylation and is inhibited by an experimental therapeutic.

A detailed model of the T7 replisome with the precise positions of the helicase and polymerase at the replication fork explains how catalysis by the two enzymes is coordinated.

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.

Human cullin-RING ligases are buffered to a much greater extent than had been previously appreciated, and the roles of ubiquitin chain extension enzymes are far more nuanced at physiological concentrations.

A mathematical model based on enzyme kinetics shows how the relationships between life expectancy, survival rates for children and adults, and national income change over time.

Mathematical analyses explore the impact of co-substrate cycling on the dynamics of cellular metabolism, and demonstrate that these dynamics can limit cellular fluxes and that co-substrate pool dynamics can be regulated to regulate fluxes.

Network symmetry represents a new vantage point for dissecting complex information processing characteristics in multisite modification, and the breaking of symmetry can confer ordering of modification and absolute concentration robustness.

Mitochondrial metabolic fluxes display a subcellular spatial gradient within a single mouse oocyte, and the fluxes are not controlled by nutrient supply or energy demand of the cell, but by the intrinsic rates of mitochondrial respiration.

Increased catalysis has been suggested to be an adaptive trait of enzymes to growth at lower temperature, but systematic analysis suggests that temperature exerts a weak selection pressure on enzyme rate enhancement, with observed variation arising from other evolutionary forces.