Aromatic amino acids

Phosphorylation is an important covalent post-translational modification (PTM) in cell

signaling pathways. This modification is a reversible process, and is catalyzed by

protein kinases. Study showed that over 30% of eukaryotic proteins are subject to

phosphorylation. Phosphorylation modification has mainly two regulatory

mechanisms for the target proteins: (1) phosphorylation may cause a conformational

change in the structure of modified proteins, such as enzymes and receptors, turning

“on” or “off” the function. (2) phosphorylation changes the proteins’ affinity to their

effector, by doing so, phosphorylated proteins can recruit or release their

downstream effectors. Hence, it is conceivable that phosphorylation modification

regulates a broad range of biological activities, such as cell growth, cell metabolism,

cell division, and so on.

Phosphorylation may occur on serine, threonine, tyrosine, and histidine residues in

eukaryotic organisms. Among these four types of phosphorylation, tyrosine

phosphorylation is most rare, but very crucial. The most famous tyrosine kinase

receptor is in the very upstream of the MAPK pathway, and regulates Ras and other

kinase, initiating the phosphorylation cascade.

Creative Proteomics has established a highly sensitive HPLC-MS/MS pipeline that

can analyze multiple kinds of phosphorylation in both eukaryotic and prokaryotic

organisms. In addition, we have optimized our protocol, enabling more fast and

sensitive site mapping service for histidine and tyrosine phosphorylation.

Learn more about aromatic amino acids at hhttps://www.creative-

proteomics.com/services/phosphorylation.htm