Magnesium-dependent adenosine triphosphatase (Mg2+-ATPase) (Mg2+-ATPase)

Magnesium-dependent adenosine triphosphatase (Mg2+-ATPase) represents a diverse class of enzymes that catalyze the hydrolysis of ATP into ADP and inorganic phosphate, strictly requiring magnesium ions as a cofactor (MeSH, Wikipedia). These enzymes are ubiquitous and reside in various cellular compartments, including the plasma membrane, mitochondria, and sarcoplasmic reticulum, where they are vital for maintaining ionic gradients and energy homeostasis (PubMed, PMC). In human physiology, specific forms such as ecto-Mg2+-ATPases (e.g., CD39/ENTPD1) play key roles in regulating extracellular nucleotide signaling, influencing both immune responses and cardiovascular function (UniProt, NIH). Altered Mg2+-ATPase activity has been linked to several pathological states, including heart failure, diabetic neuropathy, and hypertension, positioning it as both a potential biomarker and a therapeutic target (PubMed Central). While pharmacological modulation of Mg2+-ATPase is complex due to its broad expression, current research focuses on selective inhibition for cancer immunotherapy and the development of calcium-sensitizing agents to enhance myofibrillar Mg2+-ATPase activity in cardiovascular disease (ResearchGate, NCBI). Additionally, bacterial Mg2+-importing ATPases (such as MgtA) are essential for pathogen survival under magnesium-limited conditions, representing a novel target for antimicrobial drug development (Journal of Bacteriology).

Other names

Mg2+ ATPaseMagnesium-importing ATPaseCa(2+) Mg(2+)-ATPaseBasal Mg2+-ATPaseEcto-Mg2+-ATPaseENTPD1 (CD39)Myofibrillar Mg2+-ATPase

Catalytic hydrolysis of ATP to ADP and inorganic phosphate requiring magnesium as a cofactor, which regulates intracellular and extracellular nucleotide levels and facilitates magnesium transport across biological membranes.