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. 2020 Jun 23;10:10205. doi: 10.1038/s41598-020-66431-w

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Kinetic profile of Class A β-lactamase PenP with Glu166Tyr mutation. (a) The pH-dependent k_cat/K_M profile of PenP Glu166Tyr mutant measured by nitrocefin assay. (b) The time-dependent ESI-MS profile of PenP Glu166Tyr hydrolyzing cephaloridine reveals the moderately slowed hydrolytic process. E: the free enzyme (29,821 Da). ES*: the enzyme-substrate acyl adduct (30,157 Da).