CD45 PROTEIN-TYROSINE-PHOSPHATASE - DETERMINATION OF MINIMAL PEPTIDE LENGTH FOR SUBSTRATE RECOGNITION AND SYNTHESIS OF SOME TYROSINE-BASED ELECTROPHILES AS POTENTIAL ACTIVE-SITE-DIRECTED IRREVERSIBLE INHIBITORS
M. Bobko et al., CD45 PROTEIN-TYROSINE-PHOSPHATASE - DETERMINATION OF MINIMAL PEPTIDE LENGTH FOR SUBSTRATE RECOGNITION AND SYNTHESIS OF SOME TYROSINE-BASED ELECTROPHILES AS POTENTIAL ACTIVE-SITE-DIRECTED IRREVERSIBLE INHIBITORS, Bioorganic & medicinal chemistry letters, 5(4), 1995, pp. 353-356
Using fyn PTK as a template, a series of phosphopeptides 1-11 spanning
in length from 1-14 amino acids was prepared. Kinetic evaluation of 1
-11 suggest that CD45 does not have a strong preference for its N- or
C-terminal amino acids and that extended phosphopeptides are not requi
red for efficient substrate turnover.