Waas, William F. et al. published their research in Biochemistry in 2003 | CAS: 24386-93-4

Physiological Concentrations of Divalent Magnesium Ion Activate the Serine/Threonine Specific Protein Kinase ERK2 was written by Waas, William F.;Dalby, Kevin N.. And the article was included in Biochemistry in 2003.Category: tetrahydrofurans The following contents are mentioned in the article:

Extracellular regulated protein kinase 2 (ERK2) is a eukaryotic protein kinase whose activity is regulated by phorbol esters, serum, and growth factors, and displays enhanced activity in several human tumors. Despite its important biol. function, its mechanism of catalysis and mode of regulation are poorly understood. Recently, we showed that in the presence of 10 mM magnesium chloride, ERK2 phosphorylates the transcription factor Ets-1 through a random-ordered ternary-complex mechanism [Waas, W. F., and Dalby, K. N. (2002) J. Biol. Chem. 277, 12532]. Now we provide kinetic evidence that ERK2 must bind two divalent magnesium ions to facilitate catalysis at a physiol. relevant rate, because a second magnesium ion promotes both MgATP^2- binding and phosphoryl transfer. The velocity dependence on magnesium at saturating concentrations of the protein substrate, EtsΔ138, over a range of ATP^4- and Mg²⁺ ion concentrations, supports the notion that magnesium is an essential activator of ERK2. At high (≥1 mM) concentrations of ATP^4-, the velocity dependence on total Mg²⁺ is sigmoidal, but plateaus at high concentrations of free Mg²⁺, where the enzyme is fully activated. At concentrations of Mg²⁺ of ≤4 mM, the velocity dependence on ATP^4- displays a peak when the concentration of ATP^4- approaches that of total Mg²⁺ and tends to zero at high concentrations of ATP^4-, where the enzyme is predominantly unactivated. The observed velocity dependencies are consistent with the notion that ERK2·EtsΔ138 complexes and ATP^4- compete for the same pool of Mg²⁺ ions in solution No binding of ATP^4- (0-2.5 mM) by ERK2 (65 μM) can be detected using isothermal titration calorimetry at 27°, pH 8.0, and an ionic strength of 0.15 M (KCl), suggesting that the complex, MgATP^2-, is the true substrate for ERK2. In contrast, 5-iodotubericidin binds ERK2 tightly (K_d = 1 μM) and displays a competitive inhibition pattern toward MgATP^2- and a mixed pattern toward free Mg²⁺, suggesting that the binding of Mg²⁺ before MgATP^2- is not compulsory. This study involved multiple reactions and reactants, such as (2R,3R,4S,5R)-2-(4-Amino-5-iodo-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-(hydroxymethyl)tetrahydrofuran-3,4-diol (cas: 24386-93-4Category: tetrahydrofurans).

(2R,3R,4S,5R)-2-(4-Amino-5-iodo-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-(hydroxymethyl)tetrahydrofuran-3,4-diol (cas: 24386-93-4) belongs to tetrahydrofuran derivatives. Tetrahydrofurans and furans are important oxygen-containing heterocycles that often exhibit interesting properties for biological applications or applications in the cosmetic industry. Tetrahydrofuran can also be produced, or synthesised, via catalytic hydrogenation of furan. This process involves converting certain sugars into THF by digesting to furfural. An alternative to this method is the catalytic hydrogenation of furan with a nickel catalyst.Category: tetrahydrofurans

Referemce:
Tetrahydrofuran – Wikipedia,
Tetrahydrofuran | (CH2)3CH2O – PubChem