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 | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.11.8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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
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