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.

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&ndash, 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&ndash, 32. PMID 15572676.

External links


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