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- Title
Specific monitoring of Syk protein kinase activity by peptide substrates including constrained analogs of tyrosine
- Authors
Donella-Deana, Arianna; Ruzza, Paolo; Cesaro, Luca; Brunati, Anna Maria; Calderan, Andrea; Borin, Gianfranco; Pinna, Lorenzo A.
- Abstract
The ability of Syk protein tyrosine kinase (PTK) to phosphorylate peptides, where tyrosine had been replaced by conformationally constrained analogs, has been exploited to develop highly selective substrates suitable for the specific monitoring of Syk activity. In particular we have synthesized a peptidomimetic, RRRAAEDDE(L-Htc)EEV (syktide), with the 3(S)-7-hydroxy-1,2,3,4-tetrahydroisoquinoline-3-carboxyl acid residue (L-Htc) replaced for tyrosine, which is phosphorylated by Syk with remarkable efficiency (Kcat=73 min−1, Km=11 μM), while it is not affected to any appreciable extent by a number of PTKs tested so far. These properties make syktide the first choice substrate for the specific monitoring of Syk.
- Subjects
PROTEIN-tyrosine kinases; PHOSPHORYLATION; PEPTIDES; ORGANIC synthesis
- Publication
FEBS Letters, 2002, Vol 523, Issue 1-3, p48
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)02932-0