Divalent cation activators

Porous Smectite-type Materials Containing Catalytically Active Divalent Cations in Octahedral Sheets... 

This enzyme activity has been observed in myosin and actomyosin, mitochondria, microsomes, and cell membranes. In some cases magnesium ions function as an activator, in others calcium ions, and in still others, both calcium and magnesium are requited. Another form of adenosine-triphosphatase is stimulated by sodium and potassium ions and is inhibited by ouabain. Some forms of the enzyme can hydrolyse inosine triphosphate and other nucleoside-5 -triphosphates. The substrate specificity may depend upon the activating divalent cation and on the presence of monovalent cations. These enzymes are probably important components of a system responsible for facilitating cation transfer in membranes. They should not be confused with adenosine triphosphate pyrophosphatase E.C. 3.6.1.8. 

First, cobait(ll) is among its activating divalent cations (cofactors), along with Mg and Mn [44]. It was found that the enzyme couid be obtained in a cation-free state (by removing the native cation(s) bound in the active centres using EDTA treatment with subsequent dialysis), in which it loses its biocatalytic activity in the absence of divalent cations in the... 

Fungal chitin synthases are found as integral proteins of the plasma membrane and in chitosomes a divalent cation, Mg(II), is necessary for enzyme activity but neither primers nor a hpid intermediate are required. The substrate and free GlcNAc activate the allosteric enzyme. UDP, the byproduct of the enzymatic activity, is strongly inhibitory to chitin synthase however, it may be metabohzed readily to UMP by a diphosphatase. 

While E. carotovora presents endo-polygalacturonase activity (10), the only hydrolase activity found in E. chrysanthemi is an exo-deaving polygalacturonase. Polygalacturonases hydrolyse a-l,4-glycosidic bonds they are active at addic pH (between 4 and 6.5) and do not require divalent cations. An exo-polygalacturonase... 

The effect of pH and cation concentration on pectinesterase (PE) activation and permeation on 30 kD MWCO ultrafiltration (UF) membrane was evaluated. In order of increasing effectiveness, PE activity was stimulated by monovalent and divalent cations, poly amines and trivalent cations. A similar trend was observed for permeation on UF membranes. Cation addition and higher pH releases PE from an inactive complex, increases activity, and increases permeation. Higher cation concentration decreases activity and permeation. These results suggest a common mechanism is involved in PE activation and permeation. 

Cobaltites with spinel stractnre have compositions MC02O4, where M is a metal forming divalent cations, snch as zinc, cadminm, magnesinm, nickel, manganese, and divalent cobalt. In contrast to the perovskites, the cobaltites have a rather high catalytic activity already at room temperatnre. Experiments show that the activity increases with increasing spinel structure content (i.e., increasing number of Co ions) of the catalyst snrface. The trivalent cobalt ions promote the withdrawal of... 

Pyruvate kinase (PK) is one of the three postulated rate-controlling enzymes of glycolysis. The high-energy phosphate of phosphoenolpyruvate is transferred to ADP by this enzyme, which requires for its activity both monovalent and divalent cations. Enolpyruvate formed in this reaction is converted spontaneously to the keto form of pyruvate with the synthesis of one ATP molecule. PK has four isozymes in mammals M, M2, L, and R. The M2 type, which is considered to be the prototype, is the only form detected in early fetal tissues and is expressed in many adult tissues. This form is progressively replaced by the M( type in the skeletal muscle, heart, and brain by the L type in the liver and by the R type in red blood cells during development or differentiation (M26). The M, and M2 isozymes display Michaelis-Menten kinetics with respect to phosphoenolpyruvate. The Mj isozyme is not affected by fructose-1,6-diphosphate (F-1,6-DP) and the M2 is al-losterically activated by this compound. Type L and R exhibit cooperatively in... 

Preanalytical variables that affect global tests for coagulation such as prothrombin time (PT) and activated partial thromboplastin time (APTT) include the choice and concentration of anticoagulant, anticoagulant-to-blQod ratio, pH, concentration of divalent cations, hematocrit, and storage temperature, to mention a few. 

Some metals can be converted to a less toxic form through enzyme detoxification. The most well-described example of this mechanism is the mercury resistance system, which occurs in S. aureus,43 Bacillus sp.,44 E. coli,45 Streptomyces lividans,46 and Thiobacillus ferrooxidans 47 The mer operon in these bacteria includes two different metal resistance mechanisms.48 MerA employs an enzyme detoxification approach as it encodes a mercury reductase, which converts the divalent mercury cation into elemental mercury 49 Elemental mercury is more stable and less toxic than the divalent cation. Other genes in the operon encode membrane proteins that are involved in the active transport of elemental mercury out of the cell.50 52... 

MgCl2 (10 mM) increased the apparent Km (83 to 173 /am) and reduced the Vjnax (3.4 to 2.4 min-1) of triazolam 4-hydroxylation by expressed CYP3A4 [21]. However, both MgCl2 (30 mM) and CaCl2 (30 mM) significantly increased reaction rates of testosterone 6/3-hydroxylation (approximately threefold) and nifedipine oxidation (three- to six-fold) by human liver microsomes (HLMs) or recombinant CYP3A4 (reconstituted with b5 and GSH) [15]. It was suggested that divalent cation stimulation on the activity was related to involvement of b5 in CYP 3A4 reaction. 

As the divalent cation effect on CYP3A4 activity appears to be substrate dependent, the benefit of including MgCl2 (1-30 mM) in the oxidative incubation should be examined for each substrate. 

Schrag, M.L. and Wienkers, L.C. (2000) Topological alteration of the CYP3A4 active site by the divalent cation Mg2+. Drug Metabolism and Disposition The Biological Fate of Chemicals, 28, 1198—1201. 

The Fur protein from E. coli was isolated in one step due to its high affinity for metal-chelate columns loaded with zinc. In DNase footprinting experiments, the Fur protein was shown to bind DNA in the promoter region of several iron-regulated genes. The consensus sequence, called the Fur box, is GATAATGATAATCATT ATC. In vitro binding is dependent on the divalent cations Co2+ Mn2+ /s Cd2+ Cu2+ at 150 iM, while Fe2+ seemed to be less active at this concentration, probably due to oxidation to Fe3+ (De Lorenzo et al., 1987). The unspecificity for divalent metals observed in vitro shows that the cells have to select the ions transported carefully and have to balance their active concentrations. In addition, it is a caveat for the experimenter to test a hypothesis on metal-ion specificity not only in vitro, but also in vivo. 

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