transphosphorylation


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transphosphorylation

 [trans″fos″for-ĭ-la´shun]
the exchange of phosphate groups between organic phosphates, without their going through the stage of inorganic phosphates.

trans·phos·phor·y·la·tion

(trans'fos-fōr'i-lā'shŭn),
A reaction involving the transfer of a phosphoric group from one compound to another, often with the involvement of ATP, as by the action of a phosphotransferase or kinase.

transphosphorylation

/trans·phos·phor·y·la·tion/ (trans″fos-for″ĭ-la´shun) the exchange of phosphate groups between organic phosphates, without their going through the stage of inorganic phosphates.

trans·phos·phor·y·la·tion

(trans'fos-fōr-i-lā'shŭn)
A reaction involving the transfer of a phosphoric group from one compound to another, often with the involvement of adenosine triphosphate.

transphosphorylation

the exchange of phosphate groups between organic phosphates, without their going through the stage of inorganic phosphates.
References in periodicals archive ?
Thus the determination of p-nitrophenol and Pi produced in the reaction with phosphate acceptor which competes with water in the hydrolytic reaction of phosphoenzyme covalent intermediate demonstrated transphosphorylation reaction as indicated by Pi / p- nitrophenol ratio (less than 1).
Tyrosine 845 on the EGFR has been reported to be a site of transphosphorylation by Src kinase (Tice et al.
The dimers subsequently induce transphosphorylation and activate the HER-2/neu receptor (Fig.
ATP] is kept high by the transphosphorylation of ADP to ATP at the expense of the phosphagen.
In normal ALK signaling, ligand-induced homodimerization of the extracellular domains brings the tyrosine kinase domains into sufficient proximity to enable transphosphorylation and kinase activity, whereas translocations resulting in pathogenic fusion partners provide dimerization domains that are ligand-independent, leading to unregulated constitutive kinase activity.
Mutagenesis of a critical Lys882 residue to a glutamate residue abolished all evidence of kinase activity, confirming that the observed phosphorylation of Tyr-to-Phe mutants was not a transphosphorylation catalyzed by another kinase.
Dimerization, transphosphorylation, protein tyrosine kinase activation, and downstream signaling subsequently occur.
After ligand binding, KIT undergoes homodimerization, transphosphorylation of tyrosine residues in its intracellular domain, and subsequent phosphorylation of downstream members of the RAS/RAF/MAPK, JAK/STAT, and PI3K/AKT signaling pathways, thus controlling cell proliferation, apoptosis, chemotaxis, and metabolism.