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...

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Veröffentlicht in:ACS catalysis 2022-08, Vol.12 (15), p.8829-8832
Hauptverfasser: Su, Dan, Kosciuk, Tatsiana, Lin, Hening
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Kosciuk, Tatsiana
Lin, Hening
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.
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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.</description><identifier>ISSN: 2155-5435</identifier><identifier>EISSN: 2155-5435</identifier><identifier>DOI: 10.1021/acscatal.2c01818</identifier><identifier>PMID: 35966602</identifier><language>eng</language><publisher>American Chemical Society</publisher><subject>Correspondence/Rebuttal</subject><ispartof>ACS catalysis, 2022-08, Vol.12 (15), p.8829-8832</ispartof><rights>2022 The Authors. Published by American Chemical Society</rights><rights>2022 The Authors. 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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. 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title Reply to Comment on “Binding Affinity Determines Substrate Specificity and Enables Discovery of substrates for N‑Myristoyltransferases”
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