Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.25 (triphosphatase)
 1,529 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The nucleoside triphosphatase [EC 3.6.1.15] activity of actomysin and that of myosin are measured by varying the concentration of nucleoside triphosphate and that of CaCl2 or MgGl2. The results thus obtained are examined by asking a question of which is responsbile for the activity, the true substrate and the active enzyme in terms of the reaction scheme shown in p. 719. The answers found for the above question are summarized in Table I (see p. 720). It is emphasized that the summmary (Table I) corresponds very well to the fact that myosin alone does not superprecipitate in the presence of either calcium or magnesium ions, whereas actomyosin does superprecipitate in the presence of magnesium ions and not in the presence of calcium ions. Obviously, the true substrate type of reaction scheme represents a kinetic property characteristic of the superprecipitation-coupled nucleoside-triphosphatase. It is also noted of the summary (Table I) that actin is capable of not only activating Mg-nucleoside-triphosphatase but also switiching the reaction scheme from the active enzyme type to the true substrate type. It is known that trinitrophenylation of myosin results in activation of the Mg-ATPase activity of myosin. However, it is now found that trinitrophenylation is not capable of switiching the reaction scheme, that is to say that the Mg-ATPase reaction of trinitrophenyl-myosin stays with the active enzyme type of reaction scheme and that of acto-trinitrophenyl-myosin with the true substrate type of reaction scheme. Effect of actin on the function of myosin seems, therefore, very unique.
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PMID:A new kinetic property characteristic of the actomyosin-nucleoside-triphosphatase. 17 88

The effect of regucalcin, a regulatory protein of Ca2+ signaling, on guanosine triphosphatase (GTPase) activity in the nuclei of rat liver was investigated. GTPase activity was significantly increased by the addition of CaCl2 (50 microm) in the enzyme reaction mixture. This increase was not seen in the presence of trifluoperazine (25 microM), an antagonist of calmodulin, which could decrease nuclear GTPase activity, suggesting that nuclear endogenous calmodulin is involved in an increase in the enzyme activity related to Ca2+ addition. The presence of regucalcin (0.5 microM) in the enzyme reaction mixture caused a significant decrease in nuclear GTPase activity. The enzyme activity was significantly raised in the presence of anti-regucalcin monoclonal antibody (25 and 50 ng/ml) in the reaction mixture. This increase was completely abolished by the addition of regucalcin (0.5 microM). Also, the effect of regucalcin addition in increasing nuclear GTPase activity was seen in the presence of EGTA (0.1 mM), a chelator of Ca2+. The present study demonstrates that endogenous regucalcin has a suppressive effect on GTPase activity in the nuclei of rat liver.
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PMID:Suppressive effect of endogenous regucalcin on guanosine triphosphatase activity in rat liver nucleus. 1151 Apr 94