Molecular Mechanisms of Enzyme Activation by Monovalent Cations
Open accessAbstract
Regulation of enzymes through metal ion complexation is widespread in biology and underscores a physiological need for stability and high catalytic activity that likely predated proteins in the RNA world. In addition to divalent metals such as Ca 2+ , Mg 2+ , and Zn 2+ , monovalent cations often function as efficient and selective promoters of catalysis. Advances in structural biology unravel a rich repertoire of molecular mechanisms for enzyme activation by Na + and K + . Strategies range from short-range effects mediated by direct participation in substrate binding, to more distributed effects that propagate long-range to catalytic residues. This review addresses general considerations and examples.
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Enzymes requiring K+ for function constitute a smaller subset of the bound K+ pool.
“A smaller subset of the bound K+ pool includes those enzymes that require K+ for function.57”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [57]
The Abstract names enzymes active only in the presence of K+, and the Kinases section says pyruvate kinase requires K+ for catalytic activity. Neither passage establishes that these enzymes constitute a smaller subset of the bound K+ pool. (LLM, conf=0.84)
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Metals in Motion: Understanding Labile Metal Pools in Bacteria
Helmann, J. D. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00726 · Cited by 49 · see citing works
- Authors
- Gohara, D. W., & Di Cera, E.
- Affiliations
- Saint Louis University (US)
- ORCID
- Gohara, David W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2016-09
- Volume
- 291
- Issue
- 40
- Pages
- 20840-20848
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC5076497
- OpenAlex
- W2499241178
- Cited by
- 97
- References
- 0
- Citations by year
- 2026: 6 · 2025: 14 · 2024: 8 · 2023: 18 · 2022: 14 · 2021: 11 · 2020: 3 · 2019: 9 · 2018: 9 · 2017: 3 · 2016: 2
- FWCI
- 0.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (HL049413, HL073813, HL112303)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
- Keywords
- enzyme activation, monovalent cations, sodium, potassium, metal complexation, enzyme regulation, catalysis, substrate binding, long-range effects, RNA world, structural biology
- MeSH terms
- Catalysis, Cations, Monovalent, Enzymes, Potassium, Sodium
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