Fas-activated serine/threonine kinase

In enzymology, a Fas-activated serine/threonine kinase (EC 2.7.11.8) is an enzyme that catalyzes the chemical reaction

ATP + [Fas-activated serine/threonine protein] ADP + [Fas-activated serine/threonine phosphoprotein]
Fas-activated serine/threonine kinase
Identifiers
EC number2.7.11.8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Thus, the two substrates of this enzyme are ATP and Fas-activated serine/threonine protein, whereas its two products are ADP and Fas-activated serine/threonine phosphoprotein.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups protein-serine/threonine kinases. The systematic name of this enzyme class is ATP:[Fas-activated serine/threonine protein] phosphotransferase. Other names in common use include FAST, FASTK, and STK10.

References

    • Tian Q, Taupin J, Elledge S, Robertson M, Anderson P (1995). "Fas-activated serine/threonine kinase (FAST) phosphorylates TIA-1 during Fas-mediated apoptosis". J. Exp. Med. 182 (3): 865–74. doi:10.1084/jem.182.3.865. PMC 2192163. PMID 7544399.
    • Li W, Simarro M, Kedersha N, Anderson P (2004). "FAST is a survival protein that senses mitochondrial stress and modulates TIA-1-regulated changes in protein expression". Mol. Cell. Biol. 24 (24): 10718–32. doi:10.1128/MCB.24.24.10718-10732.2004. PMC 533970. PMID 15572676.


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