ArticleBiophysical journal2022
Single-molecule studies reveal method for tuning the heterogeneous activity of alkaline phosphatase.
Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 17 citations in OpenAlex.
- Anfinsen Redux: Ribonuclease Folding in the Single-Molecule Regime.Journal of the American Chemical Society · 2025Article
- Single-Molecule Enzyme Activity Analysis for Illuminating Pathological Proteoforms.ACS central science · 2025Review
- Partition-Less Digital Immunoassay Using Configurable Topographic Nanoarrays for Extracellular Vesicle Diagnosis of Ewing Sarcoma.ACS nano · 2025Article
- Dietary flavonoids form supramolecular assemblies, alter biochemistry, and enhance cell resilience.Frontiers in nutrition · 2025Article
- Digital Cascade Assays for ADP- or ATP-Producing Enzymes Using a Femtoliter Reactor Array Device.ACS sensors · 2023Article
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
Single-molecule-enzymology (SME) methods have enabled the observation of heterogeneous catalytic activities within a single enzyme population. Heterogeneous activity is hypothesized to originate from conformational changes in the enzyme that result from changes in the local environment leading to catalytically active substates. Here, we use SME to investigate the mechanisms of heterogeneous activity exhibited by tissue nonspecific alkaline phosphatase (TNSALP), which reveals two subpopulations with different catalytic activities. We show the effect of pH and temperature on the distribution of TNSALP activity and confirm the presence of two subpopulations attributed to half- and fully active TNSALP substates. We provide mechanistic insight about protein structure using molecular dynamic simulations and show pH- and temperature-dependent conformational transitions that corroborate experimentally observed changes in TNSALP activity. These results show the utility of SME to understand heterogeneous enzyme activity and demonstrate a simple approach using pH and temperature to tune catalytic activity within an enzyme population.
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