Reference work entry
MK-STYX was first identified bioinformatically due to its homology with the dual specificity phosphatases (DUSPs), a family of enzymes known for their ability to dephosphorylate not only tyrosine residues but also serine and threonine residues (Wishart and Dixon 1998). Specifically, MK-STYX resembles a MAP kinase phosphatase (MKP), which contains a rhodenase or Cdc25 homology (CH2) domain in its N-terminus, while containing a DUSP domain in its C-terminus. The name of the protein reflects this similarity, as MK-STYX was coined from the phrase MAP Kinase Phosphatase-like Serine Threonine T yrosine inter action domain (Wishart and Dixon 1998). The Ser/Thr/Tyr interaction (STYX) domain was so named based on the observation that, though this domain shares significant homology to a DUSP domain, it lacks a critical cysteine residue necessary for catalysis; the conservative substitution of a serine in place of this residue renders this enzyme...
© Springer International Publishing AG 2018