Search results
Results from the WOW.Com Content Network
Tyrosine phosphorylation is the addition of a phosphate (PO 4 3−) group to the amino acid tyrosine on a protein. It is one of the main types of protein phosphorylation . This transfer is made possible through enzymes called tyrosine kinases .
Tyrosine phosphorylation is a fast, reversible reaction, and one of the major regulatory mechanisms in signal transduction. Cell growth, differentiation, migration, and metabolic homeostasis are cellular processes maintained by tyrosine phosphorylation. The function of protein tyrosine kinases and protein-tyrosine phosphatase counterbalances ...
Tyrosine kinases belong to a larger class of enzymes known as protein kinases which also attach phosphates to other amino acids such as serine and threonine. Phosphorylation of proteins by kinases is an important mechanism for communicating signals within a cell (signal transduction) and regulating cellular activity, such as cell division.
In its phosphorylated form, tyrosine is called phosphotyrosine. Tyrosine phosphorylation is considered to be one of the key steps in signal transduction and regulation of enzymatic activity. Phosphotyrosine can be detected through specific antibodies. Tyrosine residues may also be modified by the addition of a sulfate group, a process known as ...
Dimerization of RTKs leads to autophosphorylation of tyrosine in the catalytic core of the dimer, and finally stimulation of the tyrosine kinase activity and cell signaling. [21] It is thus an example of a trans-autophosphorylation reaction, where one receptor subunit of the dimer phosphorylates the other subunit.
Serine in an amino acid chain, before and after phosphorylation. In biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion. [1] This process and its inverse, dephosphorylation, are common in biology. [2] Protein phosphorylation often activates (or deactivates) many enzymes. [3] [4]
Structure of Aurora A kinase (PDB: 3E5A) with labeled elements of secondary structure. The catalytic subunits of protein kinases are highly conserved, and the structures of over 280 of the approximately 494 kinase domains from 481 human genes have been determined, [8] leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases. [9]
A second regulatory phosphorylation site in Src is Tyr-416. This is an autophosphorylation site in the activation loop. It was found that a phosphorylation of Tyr-416 and Tyr-416 can suppressing the transforming ability of the activating Tyr-527→Phe mutation by Tyr-416→Phe mutation leads to maximal stimulation of kinase activity. [11]