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A Designed Enzyme Promotes Selective Post-translational Acylation.
Gosavi, Pallavi M; Jayachandran, Megha; Rempillo, Joel J L; Zozulia, Oleksii; Makhlynets, Olga V; Korendovych, Ivan V.
Afiliación
  • Gosavi PM; Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
  • Jayachandran M; Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
  • Rempillo JJL; Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
  • Zozulia O; Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
  • Makhlynets OV; Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
  • Korendovych IV; Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Chembiochem ; 19(15): 1605-1608, 2018 08 06.
Article en En | MEDLINE | ID: mdl-29756279
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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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Calmodulina / Procesamiento Proteico-Postraduccional / Sustitución de Aminoácidos / Lisina Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: ALEMANHA / ALEMANIA / DE / DEUSTCHLAND / GERMANY
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Calmodulina / Procesamiento Proteico-Postraduccional / Sustitución de Aminoácidos / Lisina Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: ALEMANHA / ALEMANIA / DE / DEUSTCHLAND / GERMANY