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A Designed Enzyme Promotes Selective Post-translational Acylation.

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.

SUBMITTER: Gosavi PM

PROVIDER: S-EPMC6394838 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature

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A Designed Enzyme Promotes Selective Post-translational Acylation.

Gosavi Pallavi M PM Jayachandran Megha M Rempillo Joel J L JJL Zozulia Oleksii O Makhlynets Olga V OV Korendovych Ivan V IV

Chembiochem : a European journal of chemical biology 20180621 15

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 calmo ...[more]

PMID: 29756279

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