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A Designed Enzyme Promotes Selective Post‐translational Acylation
Author(s) -
Gosavi Pallavi M.,
Jayachandran Megha,
Rempillo Joel J. L.,
Zozulia Oleksii,
Makhlynets Olga V.,
Korendovych Ivan V.
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800196
Subject(s) - calmodulin , acylation , enzyme , chemistry , chemical biology , posttranslational modification , residue (chemistry) , biochemistry , computational biology , biology , catalysis
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.