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Reply to Comment on "Binding Affinity Determines Substrate Specificity and Enables Discovery of substrates for N-Myristoyltransferases".
Su, Dan; Kosciuk, Tatsiana; Lin, Hening.
Afiliação
  • Su D; Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States.
  • Kosciuk T; Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States.
  • Lin H; Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States.
ACS Catal ; 12(15): 8829-8832, 2022 Aug 05.
Article em En | MEDLINE | ID: mdl-35966602
ABSTRACT
In our previously published article, an intriguing enzymology observation with the N-myristoyltransferases (NMT1 and NMT2) led us to conclude that binding affinity is important for determining in vivo substrate specificity and this can explain the vast literature that reports the coimmunoprecipitation of protein-modifying enzymes and their substrates. This understanding also provides a facile method to identify substrate proteins for such enzymes, which we demonstrated by identifying three substrate proteins using existing interactome data for NMT1 and NMT2. Dr. Meinnel recently commented on our finding, and we hope this Reply helps to clarify some of the important points we aimed to make in the original article.

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2022 Tipo de documento: Article