Su Dan, Kosciuk Tatsiana, Lin Hening
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States.
Howard Hughes Medical Institute; Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States.
ACS Catal. 2022 Aug 5;12(15):8829-8832. doi: 10.1021/acscatal.2c01818. Epub 2022 Jul 8.
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.
在我们之前发表的文章中,对N-肉豆蔻酰转移酶(NMT1和NMT2)进行的一项有趣的酶学观察使我们得出结论,结合亲和力对于确定体内底物特异性很重要,这可以解释大量报道蛋白质修饰酶及其底物共免疫沉淀的文献。这种认识还提供了一种简便的方法来鉴定此类酶的底物蛋白,我们通过使用NMT1和NMT2的现有相互作用组数据鉴定出三种底物蛋白来证明了这一点。梅内尔博士最近对我们的发现发表了评论,我们希望这篇回复有助于澄清我们在原始文章中旨在阐述的一些要点。