Adenosine Diphosphate-adenosine Triphosphate Exchange Research Articles

Additional effects of monovalent cations on the lysine-sensitive aspartokinase of E. coli B

The apparent specificity of activation of lysine-sensitive aspartokinase (E.C.2.7.2.4) from E. coli by monovalent cations differs depending on the assay used and on the Mg 2+ concentration. Activity is nearly absolutely dependent on and is highly specific for a monovalent cation in the aspartate semialdehyde dehydrogenase coupled assay or the adenosine triphosphate-adenosine diphosphate exchange assay. Little specificity for monovalent cations is observed using the aspartyl hydroxamate assay. Activation and specificity are also altered by Mg 2+ concentrations at a constant 5 mM nucleotide concentration. At a low ( 1.25 or 1.6 mM) Mg 2+ concentration, monovalent cation activation and specificity are nearly absolute. Less dependence on monovalent cations and less specificity are observed at a higher Mg 2+ concentration (6 mM). Li + inhibits aspartokinase competitively with respect to either K + or NH 4 +. Monovalent cations are also thermoprotective and differential thermal inactivation experiments at 56°C reveal that NH 4 + and K +, either of which will produce maximum catalytic activity, interact differently with aspartokinase. K + interacts with positive cooperativity, whereas NH 4 + does not. K +, NH 4 +, and Na + are about equally effective in enhancing the dissociation of the aspartokinase-aspartylphosphate complex. Li + is less effective.

Effects of arginine and some analogues of the partial adenosine triphosphate-adenosine diphosphate exchange reaction catalysed by arginine kinase. Evolutionary divergence in the mechanism of action of a monomer and a dimer arginine kinase

1. Both the monomer arginine kinase from lobster muscle and the dimer arginine kinase from Holothuria forskali catalyse the ATP-ADP partial exchange reaction at rates equal to 3 and 0.6% of the normal rate of transphosphorylation respectively. The Mg2+-nucleotide complex is the substrate for this as it is for the kinase reaction. 2. Analogues of arginine inhibit the exchange reaction of the lobster enzyme but enhance that of the Holothuria enzyme. 3. With the lobster enzyme NO3- has no effect on the exchange reaction alone and inhibit only slightly the apparent enhancement of the exchange reaction produced by the addition of arginine. This is compatible with previous findings for this enzyme that formation of the anion-stabilized dead-end complex, enzyme-arginine-MgADP-NO3-, does not occur to any marked degree. 4. About 80% of the ADP-ATP exchange reaction of the lobster enzyme remains after inhibition with iodoacetamide. This is further decreased to 65% by the addition of L-arginine, indicating that this substrate does bind to the thiolmodified enzyme. 5. It is concluded that the partial exchange reaction is a genuine phenomenon not mediated by trace amounts of arginine. From the effects of arginine and related compounds it would appear that during the normal kinase reaction the partial ATP-ADP exchange reaction is suppressed in the lobster enzyme but enhanced in the Holothuria enzyme. This reflects a remarkable evolutionary divergence of two homologous enzymes.

Effects of cations on the adenosine diphosphate-adenosine triphosphate exchange reaction catalyzed by rat brain microsomes

Some properties of a (Na + + Mg 2+)-dependent ADP-ATP exchange reaction catalyzed by Nal-treated rat brain microsomes have been investigaged. The (Na + + Mg 2+)-activated exchange exhibited an absolute requirement for Na +, was inhibited by ouabain and stimulated 2–3-fold by oligomycin. The optimum MgCl 2 concentration for the (Na + + Mg 2+)-activated exchange was 1.0 mM, but in the presence of oligomycin 3.0 mM MgCl 2 was required for optimum activity. The exchange reaction exhibited a complex multiphasic response to increasing concentration of Na +, with activity increasing up to 200 mM NaCl.

Effect of Potassium on Sodium-dependent Adenosine Diphosphate-Adenosine Triphosphate Exchange Activity in Kidney Microsomes

Abstract Maximal activation of a Na+-dependent adenosine diphosphate-adenosine triphosphate exchange reaction mediated by kidney microsomes was achieved at 0.1 mm and 0.4 mm Mg++ in the presence of 1.5 mm and 32 mm Na+, respectively. K+ inhibited the Na+-dependent exchange rate when lower concentrations of Na+ and Mg++ were used and stimulated it in the presence of 0.4 mm Mg++ and 32 mm Na+. The inhibitory effect of K+ could be reversed either by increasing the Na+ concentration or decreasing that of K+. N-Ethyl-maleimide treatment of microsomes abolished the stimulatory effect of K+. Ouabain, alkaline pH, and lower temperatures less effectively decreased stimulation of Na+-dependent exchange by K+. Mg++ and K+ appeared to exhibit competitive antagonism on (Na+ + K+)-sensitive transphosphorylation activity. It is proposed that the stimulation of Na+-dependent adenosine diphosphate-adenosine triphosphate exchange reaction by K+ may be mediated, in part, by slowing the conversion of one form of the phosphoenzyme E1-P into another E2-P.

Potassium ion-stimulated and sodium ion-dependent adenosine diphosphate-adenosine triphosphate exchange activity in a kidney microsomal fraction.

1. K(+) did not affect the Mg(2+)-dependent transphosphorylation but markedly increased the Na(+)-stimulated ADP-ATP exchange rate mediated by a microsomal fraction from guinea-pig kidney. 2. Rb(+), Cs(+), NH(4) (+) and Li(+) were equally effective in stimulating the Na(+)-dependent ADP-ATP exchange activity. 3. Treatment of the microsomal fraction with N-ethylmaleimide or increased concentrations of Mg(2+) prevented stimulation of the Na(+)-dependent exchange reaction by K(+). 4. Ouabain (2.5mum) inhibited ATP hydrolysis by 33% but did not decrease the K(+)-stimulated Na(+)-dependent ADP-ATP exchange rate. 5. A possible mechanism for stimulation of exchange activity by K(+) is discussed.

On the role of the adenosine diphosphate-adenosine triphosphate exchange reaction in oxidative phosphorylation: Effect of calcium

FEBS LettersVolume 7, Issue 4 p. 339-342 Full-length articleFree Access On the role of the adenosine diphosphate-adenosine triphosphate exchange reaction in oxidative phosphorylation: Effect of calcium F.L. Bygrave, F.L. Bygrave Department of Biochemistry, The Australian National University, Faculty of Science, Canberra, A.C.T., AustraliaSearch for more papers by this authorK.C. Reed, K.C. Reed Department of Biochemistry, The Australian National University, Faculty of Science, Canberra, A.C.T., AustraliaSearch for more papers by this author F.L. Bygrave, F.L. Bygrave Department of Biochemistry, The Australian National University, Faculty of Science, Canberra, A.C.T., AustraliaSearch for more papers by this authorK.C. Reed, K.C. Reed Department of Biochemistry, The Australian National University, Faculty of Science, Canberra, A.C.T., AustraliaSearch for more papers by this author First published: May 01, 1970 https://doi.org/10.1016/0014-5793(70)80200-9Citations: 9AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat References 1 F.L. Bygrave, A.L. Lehninger, J. Biol. Chem., 241, (1966), 3894– 2 F.L. Bygrave, K.C. Reed, Proc. Australian Biochem. Soc., (1969), 59– 3 C. Schnaitman, P.L. Pederson, Biochem. Biophys. Res. Commun., 30, (1968), 428– 4 W.C. Schneider, J. Biol. Chem., 176, (1948), 259– 5 J.F. Morrison, Anal. Biochem., 24, (1968), 106– 6 R.J.L. Allen, Biochem. J., 34B, (1940), 858– 7 F.L. Bygrave, unpublished observations. 8 A.L. Lehninger, The Mitochondrion (1963), Benjamin New York 95– 9 E. Racker, Mechanisms in Bioenergetics (1965), Academic Press New York 129– 10 M.G. Colomb, J.G. Laturaze, P.V. Vignais, Biochem. Biophys. Res. Commun., 24, (1966), 909– 11 R.P. Glaze, C.L. Wadkins, J. Biol. Chem., 242, (1967), 2139– 12 A. Goffeau, P.L. Pederson, A.L. Lehninger, J. Biol. Chem., 242, (1967), 1815– 13 G.S.P. Groot, S.G. van den Bergh, Biochim. Biophys. Acta, 153, (1968), 22– 14 M.E. Pullman, H.S. Penefsky, A. Datta, E. Racker, J. Biol. Chem., 235, (1960), 3322– 15 H. Zalkin, M.E. Pullman, E. Racker, J. Biol. Chem., 240, (1965), 401– 16 F.L. Bygrave, A.L. Lehninger, Proc. Natl. Acad. Sci., 51, (1967), 1409– 17 P. Mitchell, Biol. Rev., 41, (1966), 445– 18 P.L. Pederson, C. Schnaitman, J. Biol. Chem., 244, (1969), 5065– 19 S.O. Nielson, A.L. Lehninger, J. Biol. Chem., 215, (1955), 555– Citing Literature Volume7, Issue4May 01, 1970Pages 339-342 ReferencesRelatedInformation

Kinetic Studies on the Arginine Kinase Reaction

A highly purified preparation of arginine kinase from the tail muscle of the crayfish, Panulirus longipes, has been used to investigate the mechanism of the reaction. The results of initial velocity, product inhibition, and isotope exchange at equilibrium studies are consistent with the reaction having a random mechanism in which all the steps are in rapid equilibrium except those concerned with the interconversion of the central ternary complexes. They also indicate that there is formation of two dead end complexes: enzyme-MgATP-phosphoarginine and enzyme-MgADP-arginine. Values are reported for the Michaelis and dissociation constants for the reaction of substrates with various enzyme forms. It has been demonstrated that an adenosine diphosphate-adenosine triphosphate exchange reaction takes place in the absence of guanidino substrates and that an arginine-phosphoarginine exchange reaction occurs in the absence of nucleotide substrates. However, the exchange rates are slow compared with the rates of the complete reaction, and thus it would appear that only a small proportion of the reaction flux does occur through a ping-pong reaction sequence. In the reverse reaction, phosphoarginine causes marked substrate inhibition that is of the noncompetitive type.

Properties of a Nucleoside Diphosphokinase from Liver Mitochondria and Its Relationship to the Adenosine Triphosphate-Adenosine Diphosphate Exchange Reaction

A nucleoside diphosphokinase which also catalyzes an adenosine triphosphate-adenosine diphosphate exchange reaction has been extracted from bovine liver mitochondria and purified by conventional methods of protein fractionation. A comparison of the catalytic properties of the two activities indicates that both are catalyzed by the same enzyme, which is different in several respects from the nucleoside diphosphokinase previously isolated by others from rat liver and from erythrocytes. Evidence is presented that the enzyme herein described also catalyzes the dinitrophenol-sensitive ATP-ADP exchange reaction when bound to intact mitochondria and to phosphorylating submitochondrial particles.

The Kinetics and Inhibition of the Adenosine Diphosphate-Adenosine Triphosphate Exchange Catalyzed by a Purified Mitochondrial Nucleoside Diphosphokinase

Abstract The kinetic behaviour of a highly purified nucleoside diphosphokinase of bovine liver mitochondria was found to be a very complex function of the concentrations of adenosine di- and triphosphate and Mg++, as well as the pH. At low ADP and excess Mg++ concentrations, the kinetic behavior is consistent with an ordered bimolecular ping-pong mechanism in which the true substrates are MgATP and either free MgADP or ADP. The enzyme is inhibited by higher concentrations of MgADP to an extent which depends on the concentration of MgATP. The enzyme is also inhibited by high concentrations of MgATP; however, MgADP is about 50 times more inhibitory than MgATP. At high levels of MgADP, the saturation curve for MgATP becomes sigmoid, with Hill interaction coefficients approaching the integral value 2.0. It has also been found that the affinity for ADP (or MgADP) as substrate and the inhibitory activity of MgADP may vary independently with pH. Furthermore, the molecular specificity of the different nucleoside 5'-diphosphates (NDP) for maximum inhibition differs from the nucleotide specificity for the catalytic event; inhibition by any given MgNDP is also dependent on the identity of the MgNTP partner. These results indicate that the mitochondrial nucleoside diphosphokinase has certain of the properties of a regulatory enzyme and that it contains two or more binding sites for the substrates, which can function either as substrates or as inhibitors, depending on the relative concentrations of ATP, ADP, and Mg++.

Studies on Adenosine Triphosphate: Arginine Phosphotransferase: PURIFICATION AND REACTION MECHANISM

A method is described for the preparation of highly purified arginine kinase from the tail muscle of the sea crayfish, Jasus verreauxi. Initial velocity studies have been made of the arginine kinase reaction in both the forward and reverse directions. When the experimental data are plotted in double reciprocal form, families of parallel straight lines are obtained. Thus it has been concluded that the reaction mechanism is of the ping-pong type so that the product of the first reactant dissociates from the enzyme before the second substrate adds to the enzyme. The conclusions with regard to the mechanism have been confirmed by the demonstration that an adenosine diphosphate-adenosine triphosphate exchange reaction occurs in the absence of the guanidino substrates and that an arginine-phosphoarginine exchange takes place in the absence of nucleotides. Whereas a divalent metal ion is required for the adenosine diphosphate-adenosine triphosphate exchange, it appears that it is not essential for the arginine-phosphoarginine exchange. Higher concentrations of phosphoarginine have been shown to give rise to the inhibition of the reverse reaction.

Sodium- potassium requiring adenosinetriphosphatase activity. 3. Purification and properties of the adenosinediphosphate-adenosinetriphosphate exchange enzyme.

Summary The ADP-ATP exchange reaction has been studied in a partially purified fraction containing (Na + -K + )-requiring ATPase prepared from pig kidney. Similarities between exchange activity and ATPase could be shown for pH optimum, K m 's for ATP, nucleotide and divalent cation specificity. The exchange reaction is unaffected by monovalent cations and none of the inhibitors of the ATPase affect the exchange reaction. The exchange enzyme was solubilized and purified 20–30-fold. No Na + -stimulated phosphorylated intermediate is formed with the solubilized exchange enzyme after incubation with [ γ - 32 P]ATP.

The Effects of Histones and Other Polycations on Cellular Energetics: II. ADENOSINE TRIPHOSPHATASE AND ADENOSINE DIPHOSPHATE-ADENOSINE TRIPHOSPHATE EXCHANGE REACTIONS OF MITOCHONDRIA

The Effects of Histones and Other Polycations on Cellular Energetics: II. ADENOSINE TRIPHOSPHATASE AND ADENOSINE DIPHOSPHATE-ADENOSINE TRIPHOSPHATE EXCHANGE REACTIONS OF MITOCHONDRIA

Distribution of an Oligomycin-sensitive Adenosine Triphosphate-Adenosine Diphosphate Exchange Reaction and Its Relationship to the Respiratory Chain

Distribution of an Oligomycin-sensitive Adenosine Triphosphate-Adenosine Diphosphate Exchange Reaction and Its Relationship to the Respiratory Chain

The Action of Oligomycin on the Inorganic Orthophosphate-Adenosine Triphosphate and Adenosine Diphosphate-Adenosine Triphosphate Exchange Reactions of Digitonin Particles

The Action of Oligomycin on the Inorganic Orthophosphate-Adenosine Triphosphate and Adenosine Diphosphate-Adenosine Triphosphate Exchange Reactions of Digitonin Particles

Properties of the Inorganic Orthophosphate-Adenosine Triphosphate and Adenosine Diphosphate-Adenosine Triphosphate Exchange Reactions of Digitonin Particles

Properties of the Inorganic Orthophosphate-Adenosine Triphosphate and Adenosine Diphosphate-Adenosine Triphosphate Exchange Reactions of Digitonin Particles

Action of chlorpromazine. 3. Mitochondrial adenosine triphosphatase and the adenosine triphosphate-adenosine diphosphate exchange.

Action of chlorpromazine. 3. Mitochondrial adenosine triphosphatase and the adenosine triphosphate-adenosine diphosphate exchange.

The Adenosine Triphosphate-Adenosine Diphosphate Exchange Reaction of Oxidative Phosphorylation

The Adenosine Triphosphate-Adenosine Diphosphate Exchange Reaction of Oxidative Phosphorylation