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.

The convergent evolution of unusually strict substrate specificity in apicomplexan LDHs arose by classic neofunctionalization of a duplicated MDH gene via few mutations of large effect.

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.

Substrate and effector bound structures of a bacterial ribonucleotide reductase reveal the molecular basis by which substrate preference is modulated by a distal site on the enzyme.

A mathematical model of glycosylation in the Golgi apparatus to investigate how the fidelity of synthesising a complex glycan distribution at the plasma membrane depends on parameters such as the number of Golgi cisternae or enzyme specificity.

Structural biology has elucidated the mechanism of a configuration-specific enzyme that decouples D-amino acids from the translational machinery and, therefore, is involved in the enforcement of homochirality during protein synthesis.

The signaling ligand (p)ppGpp regulates the enzyme HPRT across species by binding to a novel class of conserved motif, yet its specificity is allosterically altered through evolution of enzyme oligomerization.

The biochemical basis for coupling cytoskeletal dynamics to regulated protein synthesis has been revealed.

Dcp2 C-terminal domain cis-regulatory elements collaborating with specific activators control decapping enzyme targeting and activation by orchestrating sequential assembly of distinct decapping complexes.

Theoretical study shows how enzymes can achieve substrate proofreading by taking advantage of existing molecular gradients in the cell while not being endowed with structural features typically required for proofreading.