Divergence in immunoproteasome substrate specificity and regulation from the constitutive proteasome impacts peptide cleavage quantity and the cellular capacity of the ubiquitin-proteasome system.
Assays using recombinant HIF prolyl hydroxylases did not support hydroxylation of more than 20 reported non-HIF substrates under conditions where robust HIF hydroxylation was observed.
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.
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.
The acquisition of new foreign DNA by the prokaryotic adaptive immune system CRISPR-Cas is shown to depend on the fundamental sequence specificity of the Cas1 integrase.
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.
A novel dynamic charge-charge interaction between B56 and a subset of PP2A-B56 substrates is essential for substrate specificity, dephosphorylation and, for KIF4A, binding condensin I.
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.
