Mechanistic and kinetics elucidation of Mg2+/ATP molar ratio effect on glycerol kinase

Magnesium Is a Key Regulator of the Balance between Osteoclast and Osteoblast Differentiation in the Presence of Vitamin D3

“…Some studies on the effect of Mg alloy degradation show cell mineralization induction [70,71], while most of the studies demonstrate that high Mg levels potentiate cell proliferation and inhibit osteogenic differentiation of bMSCs [72,73,74]. It is worthwhile to note that Mg 2 ATP species form at intra-cellular Mg concentration >5 mM to the detriment of MgATP 2− [9], the latter being the biological active species required for enzyme activity and, hence, cellular function. Thus, high Mg might impair the activity of one or more Mg-dependent protein kinases, which usually inhibit osteoclast differentiation and promote osteoblast differentiation in physiological conditions.…”

“…Apart from being required for DNA, RNA, and protein synthesis, Mg participates in several biochemical processes acting as a cofactor for hundreds of enzymatic reactions. MgATP 2− is both the active Mg species in enzyme binding and the energy-producing form in the cellular active transport [5,6,7,8], although multiple Mg–ATP complexes at different Mg to ATP molar ratio were described ([9] and references cited therein). Also, Mg is the second element in bone after Ca and part of the Mg on bone surface (30%) is exchangeable, acting as a dynamic store to maintain intra- and extracellular Mg levels [10,11].…”

A real-time 31P-NMR-based approach for the assessment of glycerol kinase catalyzed monophosphorylations

“…shows a maximum activity at the optimum Mg 2+ to ATP molar ratio of (0.12 – 0.3) and exhibits a two-step kinetic behavior as function of ATP at fixed Mg 2+ concentrations. Such behavior correlates with the formation of various Mg 2+ -ATP complexes that bind to the active site [9] . Thus, for a more comprehensive kinetic characterization of the glycerol kinase under study, Mg 2+ -ATP complexes at different Mg 2+ /ATP molar ratios should be considered.…”

“…Such interaction depends on the Mg 2+ to ATP molar ratio and results in the generation of Mg-ATP complexes of various physical and chemical features. Consequently, the freely accessible ATP co-substrate for the enzyme is altered, substantially affecting glycerol kinase kinetics [9] . For instance, it has been shown that glycerol kinase from Cellulomonas sp .…”

ATP line splitting in association with reduced intracellular magnesium and pH: a brain 31P MR spectroscopic imaging (MRSI) study of pediatric patients with myelin oligodendrocyte glycoprotein antibody‐associated disorders (MOGADs)

“…For example, β-ATP allows evaluation of intracellular free Mg 2+ concentration, 15,[21][22][23] since the β-ATP chemical shift is highly sensitive to Mg 2+ binding. 23,24 γ-ATP allows the assessment of ATP fluxes in the pathways of ATPase and creatine kinase by magnetization transfer, [17][18][19] owing to the kinetic reactions P i + MgADP ! MgATP and PCr + MgADP $ MgATP + Cr (P i , inorganic phosphate; ADP, adenosine diphosphate; PCr, phosphocreatine; Cr, free creatine).…”