A Designed Enzyme Promotes Selective Post-translational Acylation

Pallavi M. Gosavi; Megha Jayachandran; Joel J.L. Rempillo; Oleksii Zozulia; Olga V. Makhlynets; Ivan V. Korendovych

doi:10.1002/cbic.201800196

A Designed Enzyme Promotes Selective Post-translational Acylation

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

Research output: Contribution to journal › Article › peer-review

2 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 language	English (US)
Pages (from-to)	1605-1608
Number of pages	4
Journal	ChemBioChem
Volume	19
Issue number	15
DOIs	https://doi.org/10.1002/cbic.201800196
State	Published - Aug 6 2018

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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10.1002/cbic.201800196

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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.",

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AU - Rempillo, Joel J.L.

AU - Zozulia, Oleksii

AU - Makhlynets, Olga V.

AU - Korendovych, Ivan V.

PY - 2018/8/6

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AB - 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.

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KW - allostery

KW - calmodulin

KW - post-translational modifications

KW - protein design

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A Designed Enzyme Promotes Selective Post-translational Acylation

Abstract

Keywords

ASJC Scopus subject areas

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