Adenylate kinase (AK)

Adenylate kinase is a highly conserved phosphotransferase enzyme (EC 2.7.4.3) present in all known organisms and tissues[2][3][8]. It catalyzes the reversible transfer of phosphate groups among adenine nucleotides, specifically the interconversion of ATP, ADP, and AMP (2 ADP ⇌ ATP + AMP), which is critical for maintaining cellular energy balance[1][3][8][10]. The enzyme consists of distinct domains for binding nucleotides and undergoes significant conformational changes during catalysis[1][5]. Multiple isoforms are found in humans, with tissue- and compartment-specific functions[2]. Adenylate kinase is involved in regulating nucleotide pools, supports various cellular signaling pathways, interacts with other metabolic enzymes and protein complexes, and impacts physiological processes such as cell maturation, apoptosis, and response to metabolic stress[2][3][9]. Its dysfunction has been linked to cardiovascular disease, cancer, and certain genetic disorders, supporting its emerging role as a therapeutic target and a marker for disease diagnosis or prognosis[2][9].

Other names

ADKmyokinaseATP-AMP phosphotransferaseEC 2.7.4.3Nucleoside monophosphate kinaseAdenylkinase

Inhibition of adenylate kinase activity blocks the conversion/interconversion of AMP, ADP, and ATP, thereby disrupting nucleotide balance and cellular energy charge[8][9].