A single mutation in a regulatory protein produces evolvable allosterically regulated catalyst of nonnatural reaction

Olesia V. Moroz, Yurii S. Moroz, Yibing Wu, Alissa B. Olsen, Hong Cheng, Korrie L. MacK, Jaclyn M. McLaughlin, Elizabeth A. Raymond, Krystyna Zhezherya, Heinrich Roder, Ivan Korendovych

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

It only takes one mutation: A strategically placed single mutation in a non-enzymatic protein scaffold produced AlleyCat, a small, allosterically regulated catalyst of Kemp elimination. In only seven rounds of directed evolution the enzymatic efficiency of the original 74 amino acid residue catalyst was improved more than 220-fold to achieve a kcat value higher than that of catalytic antibodies for the same reaction, still preserving allosteric regulation.

Original languageEnglish (US)
Pages (from-to)6246-6249
Number of pages4
JournalAngewandte Chemie (International Edition in English)
Volume52
Issue number24
DOIs
StatePublished - Jun 10 2013

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Keywords

  • enzyme catalysis
  • metalloproteins
  • protein design

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis

Cite this

Moroz, O. V., Moroz, Y. S., Wu, Y., Olsen, A. B., Cheng, H., MacK, K. L., McLaughlin, J. M., Raymond, E. A., Zhezherya, K., Roder, H., & Korendovych, I. (2013). A single mutation in a regulatory protein produces evolvable allosterically regulated catalyst of nonnatural reaction. Angewandte Chemie (International Edition in English), 52(24), 6246-6249. https://doi.org/10.1002/anie.201302339