Enzyme Activity Measurement of Adenylate Kinase

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Adenylate kinase (EC 2.7.4.3, AK) is a phosphotransferase enzyme that catalyzes the reversible transfers of terminal phosphate group between adenine nucleotides. ATP is used as the donor, and AMP is the acceptor, producing two molecules of ADP. The enzyme activity highly depends on Mg²⁺. The catalyzed reaction requires a nucleotide complexed with Mg²⁺ (Mg²⁺-ATP complex) as the first substrate and a free nucleotide as the second substrate.

Adenylate kinase is essential for cellular growth and multiplication. This enzyme has abundant existences inside the cell and participates in several metabolism pathways, such as the adenosine ribonucleotides de novo biosynthesis, biosynthesis of antibiotics, and purine metabolism pathway. The indispensable positions of this enzyme reflect in metabolic motoring and energy homeostasis. In signal transductions, AK can identify the AMP metabolic signals and deliver them to metabolic sensors, thus, facilitating the decoding of cellular information. In energy metabolism, the two high-energy phosphoryls in ATP molecule can be produced by AK. Therefore, AK participates in the regulation of energy flux. Many clinical diseases are related to the deficiency of AK. For example, the deficiency in the erythrocyte will cause hemolytic anemia, which is a rare hereditary erythroenzymopathy. The clinical manifestations include mental retardation and psychomotor impairment. Noticing the clinical significances, a growing number of studies are focused on the activity detection and medical research. To facilitate such effort, Creative Enzymes offers highly sensitive and more flexible methods to satisfy different demands.

Figure: The crystal structure of wild-type adenylate kinase from E. coli, in complex with Ap5A (diadenosine pentaphosphate).
Reference: Schrank, T.P et al. Proc.Natl.Acad.Sci.USA 2009 106: 16984-16989.

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