Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of the alkaline phosphatase inhibitors levamisole and R 8231 on p-nitro-phenylphosphatase, inorganic pyrophosphatase and adenosine triphosphatase (ATPase) activities in dentingenically active odontoblasts were studied. The p-nitrophenylphosphatase and inorganic pyrophosphatase activities were inhibited, while 40% of the ATP-splitting enzyme activity remained under the assay condition used. This finding, togeather with earlier studies, indicates that at least two different phosphatase are active at alkaline pH in hard tissue-forming cells; on nonspecific alkaline phosphatase and one specific ATPase. The ATPase activity is uninfluenced by ouabain and ruthenium red and is activated by Ca-2+ ions.
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PMID:Inhibition studies of alkaline phosphatase in hard tissue-forming cells. 16 33

The characteristics of nonspecific alkaline phosphatase, (APase, EC 3.1.3.1.) measured as beta-glycerophosphatase (GPase, EC 3.1.3.1.), inorganic pyrophosphatase (PPiase, EC 3.6.1.1.) and adenosine triphosphatase (ATPase, EC 3.6.1.3.) were studied in detail of butanol extracts prepared from rat molar cementum. Mg2+ was not absolutely essential to any of the activities, but at low levels was stimulatory in all cases. Higher concentrations were inhibitory. Ca2+ stimulated ATPase activity weakly at low levels, but was slightly inhibitory to the other enzyme activities. All enzyme activities showed nearly identical sensitivities to heat inactivation and to L-p-bromotetramisole and levamisole, which caused nearly complete inhibition. About 10-15% of the ATPase activity was insensitive to L-p-bromotetramisole and levamisole. The data are consistent with the concept that GPase, PPiase and ATPase activities of cementum to a major part stem from one enzyme, namely nonspecific alkaline phosphatase.
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PMID:Properties of alkaline phosphatases from cellular cementum of rat molars. 612 76

Rhythmometric analysis of a group of phosphohydrolases in mouse liver has been performed along a single 24 hr time scale. The presence of the rhythm was conducted by F test. Statistically significant circadian rhythm was detected in glucose-6-phosphatase (G6Pase) and inorganic pyrophosphatase (InPPase) activity expressed on fresh weight and protein basis. Both G6Pase and InPPase oscillated with a high amplitude of 0.44 U and 1.15 U respectively across the mean value (mesor) of 0.40 +/- 0.42 U and 2.81 +/- 1.14 U per mg protein and with a phase shift of 80 degrees (5.34 hr) among them. On the other hand, alkaline phosphatase (AlPase) did not show any rhythm whereas adenosine triphosphatase (ATPase) showed rhythmic activity on protein basis and oscillated across mesor of 1.84 +/- 0.5 U with an amplitude of 0.52. Acrophase (time for peak activity/mg protein) of G6Pase, InPPase and ATPase was found at 194.2 degrees (13.34 hr), 114.1 degrees (8.0 hr) and at 306.1 degrees (20.4 hr) respectively. AlPase, though did not show significant rhythm, had peak value at 231.8 degrees. Since hepatic G6Pase is a multicomponent and multifunctional enzyme with several overlapping activities (viz. InPPase), coordinated action of G6Pase and InPPase in the regulation of hepatic cell functions has been suggested.
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PMID:Circadian rhythmometric analysis of hepatic phosphohydrolases with special reference to glucose-6-phosphatase and inorganic pyrophosphatase. 795 48

The activities of inorganic pyrophosphatase (PPase) and adenosine triphosphatase (ATPase) were studied in the plasma membrane of Leishmania donovani promastigotes and amastigotes. It was shown that the specific activity of PPase was greater than that of ATPase in the promastigote plasma membrane. We characterized H+-PPase present in the plasma membrane of L. donovani and investigated its possible role in the survival of promastigote and amastigote. PPase activity was stimulated by K+ and sodium orthovanadate and inhibited by pyrophosphate analogs (imidodiphosphate and alendronate), KF, N,N'-dicyclohexylcarbodiimide (DCCD), thiol reagents (p-chloromercuribenzenesulfonate (PCMBS), N-ethylmaleimide (NEM), and phenylarsine oxide (PAO)), the ABC superfamily transport modulator verapamil, and also by the F(1)F(o)-ATPase inhibitor quercetin. ATPase activity was stimulated by K+ and verapamil, inhibited by DCCD, PCMBS, NEM, sodium azide, sodium orthovanadate, and quercetin, and was unaffected by PAO. We conclude that there are significant differences within promastigote, amastigote, and mammalian host in cytosolic pH homeostasis to merit the inclusion of PPase transporter as a putative target for rational drug design.
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PMID:Membrane bound pyrophosphatase and P-type adenosine triphosphatase of Leishmania donovani as possible chemotherapeutic targets: similarities and differences in inhibitor sensitivities. 1996 21

This minireview in memory of Daniel I. Arnon, pioneer in photosynthesis research, concerns properties of the first and still only known alternative photophosphorylation system, with respect to the primary phosphorylated end product formed. The alternative to adenosine triphosphate (ATP), inorganic pyrophosphate (PPi), was produced in light, in chromatophores from the photosynthetic bacterium Rhodospirillum rubrum, when no adenosine diphosphate (ADP) had been added to the reaction mixture (Baltscheffsky H et al. (1966) Science 153: 1120-1122). This production of PPi and its capability to drive energy requiring reactions depend on the activity of a membrane bound inorganic pyrophosphatase (PPase) (Baltscheffsky M et al. (1966) Brookhaven Symposia in Biology, No. 19, pp 246-253); (Baltscheffsky M (1967) Nature 216: 241-243), which pumps protons (Moyle J et al. (1972) FEBS Lett 23: 233-236). Both enzyme and substrate in the PPase (PPi synthase) are much less complex than in the case of the corresponding adenosine triphosphatase (ATPase, ATP synthase). Whereas an artificially induced proton gradient alone can drive the synthesis of PPi, both a proton gradient and a membrane potential are required for obtaining ATP. The photobacterial, integrally membrane bound PPi synthase shows immunological cross reaction with membrane bound PPases from plant vacuoles (Nore BF et al. (1991) Biochem Biophys Res Commun 181: 962-967). With antibodies against the purified PPi synthase clones of its gene have been obtained and are currently being sequenced. Further structural information about the PPi synthase may serve to elucidate also fundamental mechanisms of electron transport coupled phosphorylation. The existence of the PPi synthase is in line with the assumption that PPi may have preceded ATP as energy carrier between energy yielding and energy requiring reactions.
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PMID:Alternative photophosphorylation, inorganic pyrophosphate synthase and inorganic pyrophosphate. 2430 71