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.
Reconstructing ancestral enzymes has revealed that a switch in kinase substrate preference evolved via an expanded specificity intermediate that is tolerated in vivo, thus providing a path for kinase diversification.
Cryo-electron microscopy structures of human ribonucleotide reductase reveal molecular details of substrate selection and allosteric inhibition through assembly of its large subunit into a ring that excludes its small subunit.
Histone-lysine N-methyltransferase SETD3 (NP_115609.2) was identified as the actin-specific histidine N-methyltransferase, an enzyme catalyzing the extremely well-conserved methylation of H73 in β-actin.
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.