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 bindi...

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Veröffentlicht in:	Chembiochem : a European journal of chemical biology 2018-08, Vol.19 (15), p.1605-1608
Hauptverfasser:	Gosavi, Pallavi M., Jayachandran, Megha, Rempillo, Joel J. L., Zozulia, Oleksii, Makhlynets, Olga V., Korendovych, Ivan V.
Format:	Artikel
Sprache:	eng
Schlagworte:	acyl transfer Acylation Allosteric Regulation allostery Amino Acid Sequence Amino Acid Substitution Animals Binding Sites Calcium-binding protein Calmodulin Calmodulin - chemistry Calmodulin - genetics Calmodulin - metabolism Humans Lysine - analysis Lysine - metabolism Models, Molecular Organic chemistry Peptides Peptides - chemistry Peptides - metabolism post-translational modifications Protein Binding protein design Protein Engineering Protein Processing, Post-Translational Proteins Sequences Translation
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