Proton demand inversion in a mutant protein tyrosine kinase reaction

Daniel M. Williams, Philip A. Cole

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


In contrast to previous studies that have shown that the neutral phenol serves as the nucleophile for WT Csk-promoted phosphorylation of a tyrosine-containing substrate, the phenolate ion acts as primary nucleophile for the D314N Csk-catalyzed reaction. Rate comparisons of D314N Csk-promoted phosphotransfer using a series of fluorotyrosine-containing peptide substrates reveal a near zero βnuc, consistent with a dissociative mechanism of phosphotransfer. These combined results argue against a hydroxy nucleophile-to-phosphate proton transfer occurring prior to an associative transition state of phosphoryl transfer.

Original languageEnglish (US)
Pages (from-to)5956-5957
Number of pages2
JournalJournal of the American Chemical Society
Issue number21
StatePublished - May 20 2002

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


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