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 Citation (Scopus)

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

Fingerprint

Acylation
Calmodulin
Enzymes
Lysine
Peptides
Catalysts
Proteins

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

Cite this

A Designed Enzyme Promotes Selective Post-translational Acylation. / Gosavi, Pallavi M.; Jayachandran, Megha; Rempillo, Joel J.L.; Zozulia, Oleksii; Makhylnets, Olga; Korendovych, Ivan.

In: ChemBioChem, Vol. 19, No. 15, 06.08.2018, p. 1605-1608.

Research output: Contribution to journalArticle

Gosavi, PM, Jayachandran, M, Rempillo, JJL, Zozulia, O, Makhylnets, O & Korendovych, I 2018, 'A Designed Enzyme Promotes Selective Post-translational Acylation', ChemBioChem, vol. 19, no. 15, pp. 1605-1608. https://doi.org/10.1002/cbic.201800196
Gosavi, Pallavi M. ; Jayachandran, Megha ; Rempillo, Joel J.L. ; Zozulia, Oleksii ; Makhylnets, Olga ; Korendovych, Ivan. / A Designed Enzyme Promotes Selective Post-translational Acylation. In: ChemBioChem. 2018 ; Vol. 19, No. 15. pp. 1605-1608.
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