Is Mg2+ sensed by adenylate kinase and serving as a signal of energy status in biological systems? (a hypothesis). Kleczkowski, L. A. & Igamberdiev, A. U. Journal of Plant Physiology, 327:154902, December, 2026. ![Is Mg2+ sensed by adenylate kinase and serving as a signal of energy status in biological systems? (a hypothesis) [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The contents of adenylates and free magnesium (Mg2+) are controlled by adenylate kinase (AK), which equilibrates specific Mg-bound and free adenylates. Taking into account the true substrates of AK, the reaction is described as: MgATP + AMPfree ↔ MgADP + ADPfree, and its equilibrium constant (K) does not depend on [Mg2+]. However, when the reaction is described in terms of total contents of adenylates, i.e., ATPtot + AMPtot ↔ 2 ADPtot, its apparent K (Kapp) varies from 0.3 to 1.5, depending on [Mg2+]. Here, we argue that Mg2+ is sensed by AK via the availability of its apparent substrates (total adenylates), and that changes in its Kapp affect internal [Mg2+]; the higher the Kapp (and energy status), the lower the [Mg2+], and vice versa. In this way, Mg2+ becomes a signal of true cellular energy charge. The Mg2+-signal controls myriad metabolic and developmental processes, including kinase reactions, photosynthesis, respiration, circadian rhythms, etc., integrating metabolism and development. The AK sensing of Mg2+ and its control over the Mg2+-signal may represent a robust and sensitive measure of energy charge. It may also be universal for any organism containing AK, with shifts in [Mg2+] as vital outputs of its activity and subsequent adenylate metabolism.
@article{kleczkowski_is_2026,
title = {Is {Mg2}+ sensed by adenylate kinase and serving as a signal of energy status in biological systems? (a hypothesis)},
volume = {327},
issn = {0176-1617},
shorttitle = {Is {Mg2}+ sensed by adenylate kinase and serving as a signal of energy status in biological systems?},
url = {https://www.sciencedirect.com/science/article/pii/S0176161726002154},
doi = {10.1016/j.jplph.2026.154902},
abstract = {The contents of adenylates and free magnesium (Mg2+) are controlled by adenylate kinase (AK), which equilibrates specific Mg-bound and free adenylates. Taking into account the true substrates of AK, the reaction is described as: MgATP + AMPfree ↔ MgADP + ADPfree, and its equilibrium constant (K) does not depend on [Mg2+]. However, when the reaction is described in terms of total contents of adenylates, i.e., ATPtot + AMPtot ↔ 2 ADPtot, its apparent K (Kapp) varies from 0.3 to 1.5, depending on [Mg2+]. Here, we argue that Mg2+ is sensed by AK via the availability of its apparent substrates (total adenylates), and that changes in its Kapp affect internal [Mg2+]; the higher the Kapp (and energy status), the lower the [Mg2+], and vice versa. In this way, Mg2+ becomes a signal of true cellular energy charge. The Mg2+-signal controls myriad metabolic and developmental processes, including kinase reactions, photosynthesis, respiration, circadian rhythms, etc., integrating metabolism and development. The AK sensing of Mg2+ and its control over the Mg2+-signal may represent a robust and sensitive measure of energy charge. It may also be universal for any organism containing AK, with shifts in [Mg2+] as vital outputs of its activity and subsequent adenylate metabolism.},
urldate = {2026-11-05},
journal = {Journal of Plant Physiology},
author = {Kleczkowski, Leszek A. and Igamberdiev, Abir U.},
month = dec,
year = {2026},
keywords = {Adenylate energy charge, Bioenergetics, Circadian rhythms, Equilibrium constant, Mg-sensing, Mg-signaling, Riboswitch (Mg)},
pages = {154902},
}
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However, when the reaction is described in terms of total contents of adenylates, i.e., ATPtot + AMPtot ↔ 2 ADPtot, its apparent K (Kapp) varies from 0.3 to 1.5, depending on [Mg2+]. Here, we argue that Mg2+ is sensed by AK via the availability of its apparent substrates (total adenylates), and that changes in its Kapp affect internal [Mg2+]; the higher the Kapp (and energy status), the lower the [Mg2+], and vice versa. In this way, Mg2+ becomes a signal of true cellular energy charge. The Mg2+-signal controls myriad metabolic and developmental processes, including kinase reactions, photosynthesis, respiration, circadian rhythms, etc., integrating metabolism and development. The AK sensing of Mg2+ and its control over the Mg2+-signal may represent a robust and sensitive measure of energy charge. 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