Fas-activated serine/threonine kinase
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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]
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.
[edit] References
- IUBMB entry for 2.7.11.8
- BRENDA references for 2.7.11.8 (Recommended.)
- PubMed references for 2.7.11.8
- PubMed Central references for 2.7.11.8
- Google Scholar references for 2.7.11.8
- 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: 865–74. 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: 10718–32. PMID 15572676.