A Designed Enzyme Promotes Selective Post-translational Acylation

Pallavi M. Gosavi, Megha Jayachandran, Joel J.L. Rempillo, Oleksii Zozulia, Olga Makhylnets, Ivan Korendovych

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

A computationally designed, allosterically regulated catalyst (CaM M144H) produced by substituting a single residue in calmodulin, a non-enzymatic protein, is capable of efficient and site selective post-translational acylation of lysines in peptides with highly diverse sequences. Calmodulin′s binding partners are involved in regulating a large number of cellular processes; this new chemical-biology tool will help to identify them and provide structural insight into their interactions with calmodulin.

Original languageEnglish (US)
Pages (from-to)1605-1608
Number of pages4
JournalChemBioChem
Volume19
Issue number15
DOIs
StatePublished - Aug 6 2018

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Keywords

  • acyl transfer
  • allostery
  • calmodulin
  • post-translational modifications
  • protein design

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

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