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. 2021 Feb 3;8:619252. doi: 10.3389/fbioe.2020.619252

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Copyright © 2021 McKenna, Balasuriya, Zhong, Li and O'Donoghue.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Normalized apparent catalytic rate (k_app) of the phosphorylation reaction catalyzed by different AKT1 phospho-forms on predicted AKT1 substrate peptides. The k_app values of each phospho-form (pAKT1^S473 (blue, open bars), pAKT1^T308 (orange, solid), and ppAKT1^T308,S473 (orange, checkered) have been normalized such that the average activity of each AKT1 variant with GSK-3β is set to 1.0. Each of the peptides shown here were individually subjected to in vitro kinase assays with each of the three AKT1 phospho-forms. Error bars represent two standard deviations about mean for three independent enzyme reactions (n = 3).