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Reply to Comment on “Binding Affinity Determines Substrate Specificity and Enables Discovery of substrates for N-Myristoyltransferases”
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 coimmunoprecipitati...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9361279/ https://www.ncbi.nlm.nih.gov/pubmed/35966602 http://dx.doi.org/10.1021/acscatal.2c01818 |
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author | Su, Dan Kosciuk, Tatsiana Lin, Hening |
author_facet | Su, Dan Kosciuk, Tatsiana Lin, Hening |
author_sort | Su, Dan |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9361279 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-93612792022-08-10 Reply to Comment on “Binding Affinity Determines Substrate Specificity and Enables Discovery of substrates for N-Myristoyltransferases” Su, Dan Kosciuk, Tatsiana Lin, Hening ACS Catal 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. American Chemical Society 2022-07-08 2022-08-05 /pmc/articles/PMC9361279/ /pubmed/35966602 http://dx.doi.org/10.1021/acscatal.2c01818 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Su, Dan Kosciuk, Tatsiana Lin, Hening Reply to Comment on “Binding Affinity Determines Substrate Specificity and Enables Discovery of substrates for N-Myristoyltransferases” |
title | Reply to Comment on “Binding Affinity Determines
Substrate Specificity and Enables Discovery of substrates for N-Myristoyltransferases” |
title_full | Reply to Comment on “Binding Affinity Determines
Substrate Specificity and Enables Discovery of substrates for N-Myristoyltransferases” |
title_fullStr | Reply to Comment on “Binding Affinity Determines
Substrate Specificity and Enables Discovery of substrates for N-Myristoyltransferases” |
title_full_unstemmed | Reply to Comment on “Binding Affinity Determines
Substrate Specificity and Enables Discovery of substrates for N-Myristoyltransferases” |
title_short | Reply to Comment on “Binding Affinity Determines
Substrate Specificity and Enables Discovery of substrates for N-Myristoyltransferases” |
title_sort | reply to comment on “binding affinity determines
substrate specificity and enables discovery of substrates for n-myristoyltransferases” |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9361279/ https://www.ncbi.nlm.nih.gov/pubmed/35966602 http://dx.doi.org/10.1021/acscatal.2c01818 |
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