Adenosine Kinase - Biochemical Properties

Biochemical Properties

AdK is a monomeric protein (~ 38-40 kDa), which works via an ordered Bi-Bi reaction mechanism. It belongs to the phosphofructokinase B (PfkB) family of sugar kinases. Other members of this family (also known as the RK family) include ribokinase (RK), inosine-guanosine kinase, fructokinase, and 1-phosphofructokinase. The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs. The structures of AdK and several other PfK family of proteins have been determined from a number of organisms (see section below) as well as that for RK protein from E. coli. Despite low sequence similarity between AdK and other PfkB family of proteins, these proteins are quite similar at structural levels. Compounds that are substrates for AdK include the N-nucleosides toyocamycin, tubercidin and 6-methylmecaptopurine riboside; the C-nucleosides formycin A, 9-azadenosine, and a large number of other C- and N-nucleoside analogs. The AdK from mammalian sources, in addition to carrying out ATP-dependent phosphorylation of Ado, also catalyzes an Ado-AMP exchange reaction requiring ADP. This activity is an integral part of AdK and it presumably allows a rapid and precise control of Ado concentration in cells. The enzymatic activity of AdK from different sources show a marked dependence on phosphate (Pi) and/or pentavalent ions and it is a conserved property of the PfkB family of proteins. The conserved NXXE motif, which is a distinctive property of the PfkB family of proteins, is involved in Pi (PVI) dependency.

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