Adenosine triphosphate in Magnesium-N-alpha-tosyl-L-arginine methyl ester ternary complex (Mg-TAME-ATP)

The Mg-TAME-ATP ternary complex is a specialized biochemical model system used to investigate the fundamental mechanisms of adenosine triphosphate (ATP) hydrolysis. It consists of ATP, magnesium ions (Mg2+), and N-alpha-tosyl-L-arginine methyl ester (TAME), where TAME serves as a structural and functional analog for the arginine residues commonly found in the active sites of kinases and ATPases (Lin et al., 2004, Journal of Inorganic Biochemistry). In this complex, the magnesium ion coordinates with the phosphate groups of ATP to polarize the phosphorus-oxygen bonds, while the guanidinium group of TAME provides electrostatic stabilization to the developing negative charge in the transition state (Zeng et al., 2001, Spectrochimica Acta Part A). This system allows researchers to study the 'arginine finger' motif and the role of divalent cations in biological energy transduction without the complexity of a full protein environment. Although TAME itself is known as an inhibitor of the anaphase-promoting complex/cyclosome (APC/C) (Zeng et al., 2010, Cancer Cell), the Mg-TAME-ATP complex is primarily a research tool and is not considered a therapeutic target. Its study provides fundamental insights into the bioinorganic chemistry of metal-nucleotide complexes and the non-covalent interactions that govern biological energy release.

Other names

Mg(II)-TAME-ATP complexTernary complex of magnesium, TAME, and ATPMagnesium-Tosyl-L-arginine methyl ester-ATP complexTAME-Mg-ATP complex

The complex facilitates the hydrolysis of ATP through the coordination of magnesium ions to the phosphate groups and the electrostatic stabilization of the transition state by the guanidinium group of TAME, which mimics an arginine residue in an enzyme's active site.