Protein phosphorylation is a reversible post-translational modification. Nine of the 20 natural
amino acids in proteins can be phosphorylated, but most of what we know about the roles of …

Cells synthesize proteins using 20 standard amino acids and expand their biochemical
repertoire through intricate enzyme-mediated post-translational modifications (PTMs). PTMs …

Histidine phosphorylation is an important and ubiquitous post-translational modification.
Histidine undergoes phosphorylation on either of the nitrogens in its imidazole side chain …

Bacterial pathogens rely on a complex network of regulatory elements to adapt to hostile
and nutrient-limiting host environments. The phosphoenolpyruvate phosphotransferase …

Background Protein histidine phosphorylation (pHis) plays critical roles in prokaryotic signal
transduction pathways and various eukaryotic cellular processes. It is estimated to account …

Actin histidine Nτ‐methylation by histidine methyltransferase SETD3 plays an important role
in human biology and diseases. Here, we report integrated synthetic, biocatalytic …

The description of the phosphate group and its reactions with nitrogen species appears to
be challenging using semi-empirical quantum chemical methods, and this holds for DFTB3 …

Protein N-phosphorylation is increasingly recognized as a critical post-translational
modification in central metabolism and cell signaling. However, other functions of N …

Post-translational modifications (PTMs) are invaluable regulatory tools for the control of
catalytic functionality, protein-protein interactions, and signaling pathways. Historically, the …

N-phosphorylation modifications are crucial for prokaryotic signal transduction and verified
as intermediate for several metabolic enzymes, yet the landscape of N-phosphorylation …