Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The cyclic peptide phalloidin, one of the toxic components of Amanita phalloides prevented the drop of viscosity of F-actin solutions after the addition of 0.6 M KI and inhibited the ATP splitting of F-actin during sonic vibration. The data concerning ATP splitting are consistent with the assumption (a) that only 1 out of every 3 actin units of the filaments needs to be combined with phalloidin in order to suppress the contribution of these 3 actins to the ATPase activity of the filament and (b) that all actin units of the filaments can combine with phalloidin with a very high affinity. -halloidin did not only stabilize the actin-actin bonds in the F-actin structure but it also increased the rate of polymerization of G-actin to F-actin. The ability of F-actin to activate myosin ATPase was not affected by phalloidin. The tropomyosin-troponin complex did not prevent the stabilizing effect of phalloidin on the F-actin structure.
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PMID:Interaction of actin with phalloidin: polymerization and stabilization of F-actin. 12 84

The slow anterior latissimus dorsi (ALD) muscles of newly hatched chickens were transposed and cross0innervated by the mixed, predominantly fast superior brachialis nerve, and investigated 2 to 15 months after the operation. Two months after the operation, myosin ATPase activity of the cross-innervated ALD muscles was still as low as in the control ALD, although the ultrastructure and the histochemical ATPase activity already showed a mixed fibre-type pattern with a predominance of fast -type fibres around the site of nerve implantation. The change of myosin properties of thw whole cross-innervated ALD did not occur until the third month after the operation. At that time, the myosin ATPase activity increased about 2.5 times and light chains of myosin of the fast type appeared in the electrophoretic pattern. The myosin ATPase activity attained 62% of the activity found in the control fast posterior latissimus dorsi muscles at three months; subsequently it remained at about this level reaching 68% 18 months after the operation. The results indicate that approximately two thirds of the cross-innervated ALD muscle fibres became changed towards the fast type under neural influence, whereas about one third remained slow, being re-innervated by the slow-type motor fibres of the implanted nerve.
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PMID:The onset and progress of transformation of avian slow into fast muscles under neural influence. 12 64

G-actin has been nitrated with tetranitromethane in conditions that lead to the modification of one tyrosine residue. The reactive residue was found by earlier workers to be Tyr-69. The nitrated actin is conformationally similar to native G-actin, as judged by sedimentation velocity and circular dichroism analysis. A small proportion only is in the form of covalently linked dimers and trimers. The nitrated G-actin will polymerise to form filaments, indistinguishable in the electron microscope from those of native F-actin, but the polymerisation process is slower. Reduction of the nitrophenol group to the corresponding aminophenol leaves the properties of the protein in respect of polymerisation unchanged. When a dansyl group is introduced at the same point, however, the ability of the actin to polymerise is lost. The nitrated actin and its reduced counterpart will also bind heavy meromyosin, and the characteristic arrowhead formation of the bound molecules along the filaments can be seen in the electron microscope. Neither of the modified F-actins, however, significantly activates or inhibits the myosin ATPase activity. The fluorescence of nitrated actin is strongly quenched through the presence of the nitrophenol chromophore. In soluble complexes with heavy meromyosin the fluorescence is indistinguishable from the sum of the separate contributions of the two protein components. There is thus no measurable excitation transfer between any tryptophan residues on the myosin heads, such as that inferred to be present in the ATPase site, and the nitrotyrosine in position 69 of the actin sequence. Implications of this observation are considered in relation to the different interaction sites in myosin and in actin. The activation of heavy meromyosin ATPase by copolymers containing actin and nitroactin in different proportions has been measured, and is not proportional to the fraction of native actin. The results are consistent with the view that the function of actomyosin depends on the interaction of the myosin heads with more than one actin subunit.
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PMID:Effects of specific chemical modification of actin. 12 59

Mild pulmonic stenosis was performed in dogs to evaluate the effect of systolic pressures overloading on the activity and subunits of myosin in the early hypertrophied right ventricle. Three weeks following pulmonary constriction, six hypertrophied dogs were sacrificed and compared to six sham-operated dogs which served as controls. In the right ventricular free wall of hypertrophied right ventricles (HRV), the heart/body weight was 46% greater than that of normal right ventricles (NRV) (p less than 0.01). Myosin ATPase activity (Vmax values) in mumoles phosphate/mg/min, was elevated significantly in the stressed ventricle for both K+ and Ca++ activity in hypertrophied right ventricles. Associated with the increase in myosin activity, there was an increase in proportion of heavy to light chains in myosin from HRV. There were approximately 2 moles of myosin light chains per mole of myosin heavy chains in NRV and approximately 1 mole of myosin light chains per mole of myosin heavy chains in HRV. The proportion of light chain C1 to C2, did not change in myosin from NRV and HRV. Of the C1 light chains, according to two-dimensional gel electrophoresis, there was less C1d as compared to C1c in HRV as compared to NRV. Thus K+- and Ca++- activated myosin is elevated in early canine HRV by pressure overload. It is suggested taht the augmented myosin activity is due to a reduction of light chain inhibition of myosin ATPase activity, which appears to result from the slower turnover rate of myosin light chains relative to heavy chains. Furthermore, when myosin light chains are added to hypertrophied right ventricular myosin, the ATPase activity is lowered.
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PMID:Modulation of myosin in right ventricular hypertrophy. 12 38

70 human hearts were studied less than 36 hours after death. The apex, and in some cases other parts of the myocardium were homogenized, DNA, hydroxyproline content, myofibrillar Ca2+ and Mg2+ ATPase were measured. In normal hearts the DNA and collagen content were 372 +/- 9 mg and 36 +/- 7 mg. Ca2+ and Mg2+ ATPase of the myofibrils prepared from these hearts have shown the same specific activity (35 +/- 5 and 34 +/- 6 nmol/min./mg) as those from fresh biopsies taken during open-chest surgery. The heart weight correlates with the DNA content (r= + 0.58 -p less than 0.01) and with the myofibrillar ATPase (r= - 0.33 - p less than 0.02) but not with the DNA concentration nor with the collagen content or concentration. The main result of this study was the presence of a negative correlation between the DNA content of the heart and the Mg2+ or Ca2+ myofibrillar ATPase (r= - 0.31, p less than 0.05 - r= - 0.45, p less than 0.01). This correlation was analysed with reference to the histological and biochemical studies published by several authors in human or experimental heart hypertrophy and it was suggested that in human heart hypertrophy the decrease of the myofibrillar or myosin ATPase is a direct consequence of the high degree of polyploidy of the muscular cells observed in this condition.
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PMID:Myofibrillar ATPase, DNA and hydroxyproline content of human hypertrophied heart. 13 Feb 42

The effects of D2O on the elementary steps in the contractile and transport ATPase [EC 3.6.1.3] reactions were studied, and the following results were obtained: 1. The rate of H-meromyosin ATPase in the steady state decreased in D2O to 60% of that in H2O. Deuterium oxide did not affect the size or rate of the initial burst of Pi liberation, i.e. the amount or rate of formation of the reactive myosin-phosphate-ADP complex, MADPP. Moreover, neither the rate of change in the fluorescence spectrum of H-meromyosin induced by ATP (the rate of formation of the second enzyme-ATP complex, M2ATP) nor the rate constant of decomposition of MADPP into M degrees + ADP + Pi was affected by D2O. However, the equilibrium constant of the step M2ATP in equilibrium MADPP decreased in D2O to about 1/2 the value in H2O. 2. In the case of the Na+-K+-dependent ATPase reactin, neither the rate constant of formation of the second enzyme-ATP complex, E2ATP, nor that of decomposition of a phosphorylated intermediate, EADP approximately P, was affected by D2O. However, the equilibrium constant of the step E2ATP in equilibrium EADP approximately P decreased in D2O to about 1/2.5-1/4 of the value in H2O. These results suggest a similarity between the modes of binding of phosphate in MADPP in the myosin ATPase reaction and in EADP approximatley P in the Na+-K+-dependent ATPase reaction.
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PMID:Effects of deuterium oxide on elementary steps in the ATPase reaction. Evidence for the similarity of key intermediates in contractile and transport ATPase. 13 92

The interaction between paramyosin and myosin has been studied by enzymological methods. Clam adductor paramyosin inhibits the actin-activated, Mg2+-requiring ATPase of both clam adductor and rabbit skeletal muscle myosins. Myosin and paramyosin must be rapidly coprecipitated for this inhibition. Incubation with F-actin in the absence of ATP does not alter this effect. This inhibition follows a hyperbolic function with respect to paramyosin concentration. Slow precipitation by dialysis of myosin and paramyosin together leads to copolymers with actin-activated ATPase equivalent to that of slowly formed myosin filaments. Both kinds of slowly formed filaments have enzymatic properties distinct from those of the rapidly precipitated proteins. Paramyosin is competitive with F-actin for their effects upon myosin. The apparent affinity of myosin for F-actin is markedly reduced by association with paramyosin, but the extrapolated maximal velocity of actomyosin is unaffected. The specificity of this inhibition is strongly suggested by marked quantitative differences between native and cleaved paramyosins. No inhibition of intrinsic myosin ATPase by paramyosin is seen. These studies suggest that at least two types of condition-dependent association between myosin and paramyosin are possible. One class of interactions is associated with enzymic inhibition in rapidly coprecipitated filaments, whereas slowly formed cofilaments exhibit catalytic activity similar to that of identically treat-d myosin and have a characteristic 14.5 nm axial repeat.
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PMID:Myosin-paramyosin cofilaments: enzymatic interactions with F-actin. 13 57

Ca2+ATPase activity and light chains of myosin, fractionated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, in developing, adult and denervated fast, slow and cardiac muscles of the rat, guinea-pig, cat, rabbit and chick were studied. It has been shown that in normal adult muscles the electrophoretic pattern of light chains of myosin reflects the myosin ATPase activity only when muscles from the same animal species are compared. In homologous muscles from adult animals differing in size, the size-dependent difference in myosin ATPase activity is not revealed in the electrophoretic pattern. Both in developing and in denervated muscle, changes in myosin ATPase activity are either connected with changes in the pattern of light chains of myosin or this pattern does not change. This relation is different in fast and slow muscles and also differs in chick and rabbit muscles. There are several possibilities of explaining the relation between ATPase activity of myosin and the pattern of light chains of myosin. The observation that myosin from the soleus muscle of 1-month-old rabbit contains light chains corresponding to both fast and slow type of myosin, indicates that the change in myosin ATPase activity during development is due to changes in the ratio between the fast and slow type of myosin.
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PMID:The relation between ATPASE activity and light chains of myosin in developing, adult and denervated muscles of several animals species. 13 84

The effects of a moderate physical training program on the hearts of rats have been studied. The mechanical responses of these hearts are improved. Possible contributing factors in this improvement are increased coronary reserve and capacity to deliver oxygen to the myocardium, increased myocardial glycogen stores and increased turnover of fatty acids through the endogenous triglyceride pool. Myocardial oxidative compounds and high energy phosphate stores are not altered. Major changes are found in the energy utilization pathways. Actomyosin, myosin, and heavy meromyosin ATPase activity and binding activity of isolated sarcoplasmic reticulum are all enhanced. Sulfhydryl control of the active site of myosin ATPase is altered. The biochemical effects of conditioning are short lived when training is decreased or discontinued.
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PMID:Effects of physical training and detraining on intrinsic cardiac control mechanisms. 13 72

The effect of 5-hydroxytryptamine (5HT) on the ATPase activity and sulphydryl group reactivity of mammalian skeletal muscle actomyosin has been studied. 5HT inhibited the Mg2+-activated but not the Ca2+-activated ATPase activity of actomyosin. It slightly activated myosin ATPase. The sulphydryl groups of actomyosin reacting with 5,5'-dithiobis-(2-nitrobenzoic acid) were blocked by concentrations of 5HT which inhibited the Mg2+-activated ATPase. The significance of the results are discussed in relation to the muscle lesions in the experimental myopathy induced by 5HT and imipramine.
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PMID:Inhibition of actomyosin ATPase by high concentrations of 5-hydroxytryptamine. Possible basis of lesion in 5HT-induced experimental myopathy. 13 9


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