An adaptor domain-mediated autocatalytic interfacial kinase reaction

Xiaoli Liao, Jing Su, Milan Mrksich*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


This paper describes a. model system for studying the autocatalytic phosphorylation of an immobilized substrate by a. kinase enzyme. This work uses self-assembled monolayers (SAMs) of alkanethiolates on gold to present the peptide substrate on a. planar surface. Treatment of the monolayer with AbI kinase results in phosphorylation of the substrate. The phosphorylated peptide then serves as a. ligand for the SH2 adaptor domain of the kinase and thereby directs the kinase activity to nearby peptide substrates. This directed reaction is intramolecular and proceeds with a. faster rate than does the initial, intermolecular reaction, making this an autocatalytic process. The kinetic non-linearity gives rise to properties that have no counterpart in the corresponding homogeneous phase reaction: in one example, the rate for phosphorylation of a mixture of two peptides is faster than the sum of the rates for phosphorylation of each peptide when presented alone. This work highlights the use of an adaptor domain in modulating the activity of a. kinase enzyme for an immobilized substrate and offers a. new approach for studying biochemical reactions in spatially inhomogeneous settings.

Original languageEnglish (US)
Pages (from-to)12303-12309
Number of pages7
JournalChemistry - A European Journal
Issue number45
StatePublished - 2009


  • Adaptor domain
  • Autocatalysis
  • Enzymes
  • Interfaces
  • Phosphorylation

ASJC Scopus subject areas

  • Catalysis
  • Organic Chemistry


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