A Designed Enzyme Promotes Selective Post‐translational Acylation

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. An allosterically regulated, computationally designed catalyst produced by substituting a single residue in calmodulin is capable of efficient and site selective post‐translational acylation of lysines in peptides with highly diverse sequences. This new tool should help to identify calmodulin′s binding partners and provide structural insight into their interactions.