Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Uniformly 32P-labeled polyribonucleotides of high specific activity can be rapidly and easily synthesized from commercially available ribonucleoside 5'-[alpha-32P]triphosphates by using two enzymes in sequence. Myosin ATPase completely and irreversibly converted any triphosphates to diphosphates in 10 min. The product diphosphates, without purification, can be polymerized by polynucleotide phosphorylase (PNPase) in 1 h with an average yield of 60%. By choosing the desired molar ratio of radioactive and nonradioactive tri- or diphosphates, polymers of a wide range of specific activity can be obtained. Since myosin ATPase and PNPase both have little base specificity, the method can be used to synthesize a radiolabeled polymer of any desired base composition.
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PMID:Enzymatic synthesis of uniformly 32P-labeled polyribonucleotides and high-specific-activity ribonucleoside 5'-[alpha-32P]diphosphates. 315 30

A Mg(2+)+Na(+)+K(+)-stimulated adenosine triphosphatase (ATPase) preparation was isolated from rat ventral prostate by flotation of microsomal membranes in high-density sucrose solutions. The reaction medium for optimum Na(+)+K(+)-stimulated ATPase activity was found to be: Na(+), 115mm; K(+), 7-10mm; Mg(2+), 3mm; ATP, 3mm; tris buffer, pH7.4 at 38 degrees , 20mm. The average DeltaP(i) (Mg(2+)+Na(+)+K(+) minus Mg(2+)+Na(+)) was 9mumoles/mg. of protein/hr., representing a 30% increase over the Mg(2+)+Na(+)-stimulated ATPase activity. At high concentrations, K(+) was inhibitory to the enzyme activity. Half-maximal inhibition of Na(+)+K(+)-stimulated ATPase activity was elicited by ouabain at 0.1mm. The preparation exhibited phosphatase activity towards ribonucleoside triphosphates other than ATP. However, stimulation of P(i) release by Na(+)+K(+) was observed only with ATP as substrate. The apparent K(m) for ATP for Na(+)+K(+)-stimulated activity was about 0.3x10(-3)m. Ca(2+) inhibited only the Na(+)+K(+)-stimulated ATPase activity. Mg(2+) could be replaced by Ca(2+) but then no Na(+)+K(+) stimulation of ATPase activity was noticed. The addition of testosterone or dihydrotestosterone (17beta-hydroxy-5alpha-androstan-3-one) in vitro at 0.1-10mum under a variety of experimental conditions did not significantly increase the Na(+)+K(+)-stimulated ATPase activity. The enzyme preparations from prostates of orchidectomized rats, however, exhibited a drastic decrease in the specific activity of Na(+)+K(+)-stimulated ATPase; these changes were prevented in the orchidectomized rats by injection of testosterone propionate.
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PMID:Studies on the microsoml sodium-plus-potassium ion-stimulated adenosine triphosphatase system in rat ventral prostate. 424 88

The presence of adenosine triphosphate, guanosine triphosphate, cytosine triphosphate, or uridine triphosphate reduced the rate of inactivation of vaccinia when heated at 50 C. The virus-associated nucleoside triphosphate phosphohydrolases (adenosine triphosphatase, guanosine triphosphatase, cytosine triphosphatase, and uridine triphosphatase) and ribonucleic acid polymerase were also protected from heat inactivation by these compounds. These obervations are best explained by postulating that ribonucleoside triphosphates bind to enzymes in the virus particle, and that these enzyme-substrate complexes are more resistant to thermal denaturation than are the enzymes without their substrates. The kinetics of heat inactivation of the vaccinia ATP phosphohydrolase activity is biphasic, suggesting that there are two proteins in the vaccinia particle that have this enzyme activity but they have different kinetics of heat inactivation. Any of the vaccinia-associated nucleotide phosphohydrolase activities are protected from heat inactivation by the presence of any one of the respective nucleoside triphosphates. This observation suggests that there is a single enzymatic site in vaccinia that is able to react with any ribonucleoside triphosphate.
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PMID:Protection of vaccinia from heat inactivation by nucleotide triphosphates. 431 59

Preparations of E. coli dnaB gene product contain ribonucleoside triphosphatase activity that is stimulated 10-fold by DNA. The products of the triphosphatase activity are nucleoside diphosphates and P(i). The dnaB complementing activity in the varphiX174 DNA-dependent system and these triphosphatase activities copurify over the last 20-fold of an extensive (about 40,000-fold) purification procedure. Acrylamide gel electrophoresis of the purified material shows a single band of protein coincident with eluted dnaB complementing and DNA-dependent and -independent nucleoside triphosphatase activities.
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PMID:Association of DNA-dependent and -independent ribonucleoside triphosphatase activities with dnaB gene product of Escherichia coli. 436 33

DNA-dependent ATPases have been purified from logarithmically growing KB cells by chromatography on single-stranded DNA cellulose and phosphocellulose. Phosphocellulose resolved the DNA-dependent ATPases into three activities designated ATPase I, II and III, respectively. From gel filtration and sedimentation analysis ATPases II and III were found to be very similar, both with calculated molecular weights of 78,000. Due to the extreme lability these enzymes were not purified further. The molecular weight of ATPase I determined by gel filtration and sedimentation analysis was calculated to be 140,000. ATPase I was further purified by gradient elution on ATP-agarose, revealing two peaks of activity (IA and IB), and by sucrose gradient sedimentation. Analysis of the fractions from the sucrose gradient by sodium dodecylsulphate gel electrophoresis revealed only one broad polypeptide band co-sedimenting with both ATPase IA and ATPase IB. This band was composed of four closely spaced polypeptides with apparent molecular weights of 66,000, 68,000, 70,000 and 71,000. Comparison of the native molecule weight (140,000) with these results suggests that ATPase I is a dimer. ATPase IA and IB were indistinguishable in their structural and enzymatic properties and presumably represent the same enzyme. The purified enzyme has an apparent Km of 0.5 mM for ATP producing ADP + Pi. A maximum activity of 2,100 molecules of ATP hydrolyzed per enzyme molecular per minute was found. Hydrolysis of ATP requires the presence of divalent cations (Mg2+ greater than Ca2+ greater than Mn2+ greater than Co2+). A broad pH optimum (pH 6--8) was observed. The enzyme uses ATP or dATP preferentially as a substrate, while other deoxyribonucleoside or ribonucleoside triphosphates were inactive. ATPase I prefers denatured DNA as cofactor. The activity with native DNA is 40% of that with denatured DNA.
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PMID:Purification and characterization of DNA-dependent ATP phosphohydrolases from KB cells. 611 62

Guanosine triphosphatase (GTPase) activity was studied histo- and cytochemically in the rod outer segments of the rat retina by means of a newly developed method. Differences in the distribution pattern of the enzyme activity exist within the outer segment: the activity is more intense at the tip of the rod outer segments near the pigment epithelium than in their proximal portion. Ultracytochemically, the new procedure reveals the reaction product of GTPase activity partly (i) on the extradisk membrane side and (ii) on the disk membranes. This result is in contrast to the cytochemical localization of guanylate cyclase (GCLase), an enzyme also localized at the tip of the rod outer segments: GCLase activity is restricted to the intradisk membrane area of the rod outer segments. The functional role of GTPase activity in the outer segments of rods is discussed.
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PMID:Histo- and cytochemical demonstration of guanosine triphosphatase activity in the outer segments of rods in the rat retina by means of a newly developed method. 613 70

Two nucleic acid-dependent ATPases have been isolated from hypotonic extracts of rat liver nuclei and partially characterized. Both enzymes are active with RNA and DNA but are most active with RNA. The most abundant enzyme, ATPase I, is a microheterogeneous, monomeric protein that consists of at least three forms with apparent molecular weights from 53,000 to 60,000. It specifically catalyzes the hydrolysis of ATP (or dATP) to ADP (or dADP) and Pi in the presence of Mg2+ ions and nucleic acid cofactor and has a Km for ATP of 0.15 mM. The other enzyme, ATPase II, consists of a single protein with an apparent molecular weight of 37,000. It catalyzes the hydrolysis of all 4 ribonucleoside triphosphates and dATP to the corresponding nucleoside diphosphate and Pi. For both enzymes, nuclear ribonucleoprotein RNA and cytoplasmic poly(A+) RNA are particularly effective cofactors, while total polysomal RNA (primarily rRNA) is a poor cofactor. The properties of these enzymes make them appear similar to other eukaryotic nucleic acid-dependent ATPases that have been isolated but distinct from the prokaryotic enzyme, RNA synthesis termination factor rho. The biological role of these enzymes is unknown.
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PMID:Two ribonucleic acid-dependent nucleoside triphosphate phosphohydrolases from rat liver nuclei. 613 77

Four chromatographically distinct DNA-dependent ATPases, B, C1, C2, and C3, have been partially purified from mouse FM3A cell extracts. These ATPases are distinguished from each other by their physical and enzymological properties. DNA-dependent ATPases B, C1, C2, and C3 have sedimentation coefficients in 250 mM KCl of 5.5, 5.3, 7.3, and 3.4 S, respectively. ATPases B, C2, and C3 hydrolyze dATP as efficiently as ATP, whereas C1 does not. ATPase B hydrolyzes other ribonucleoside triphosphates with relatively high efficiency as compared to the other three enzymes. ATPase C3 prefers poly[d(A-T)] to poly(dT) as cofactor, whereas the other three enzymes prefer poly(dT) to poly[d(A-T)]. Among the four ATPases, ATPase C3 has been highly purified and characterized in detail. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the most purified fraction of ATPase C3 showed two major bands corresponding to molecular weights of 66 000 and 63 000. The Km values of the enzyme for ATP and dATP are 0.53 and 0.86 mM, respectively. As cofactor, poly[d(A-T)] is the most effective among the DNAs tested. Heat-denatured DNA and native DNA are also effective but used with less efficiency. Almost no or very little activity has been detected with ribohomopolymers and oligonucleotides. The activity attained with poly(dT) and poly(dA) is 11 and 6% of that with heat-denatured DNA, respectively. When both polymers were added at a molar ratio 1 to 1, very high activity was obtained with these polymers. On the other hand, little activity was observed by the combination of noncomplementary homopolymers such as poly(dT) and poly(dG).
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PMID:Multiple deoxyribonucleic acid dependent adenosinetriphosphatases in FM3A cells. Characterization of an adenosinetriphosphatase that prefers poly [d(A-T)] as cofactor. 614 25

The product of bacteriophage P22 gene 12 is known from genetic experiments to be essential for phage DNA replication. The P22 12 protein has been purified to near homogeneity from Escherichia coli lysogenic for lambda-P22 hybrid phage containing the replication genes of P22. The protein has a subunit molecular weight of 46,000. The purified protein contains ATPase activity that is stimulated by single-stranded DNA. The ATPase is poorly stimulated by double-stranded DNA. All four ribonucleoside triphosphates are hydrolyzed; none of the deoxynucleoside triphosphates are hydrolyzed. In addition, the P22 12 protein binds to single-stranded DNA in the presence of ATP. Studies of oligonucleotide synthesis by P22 12 protein in conjunction with E. coli dnaG primase are presented in the succeeding paper (Wickner, S. (1984) J. Biol. Chem. 259, 14044-14047).
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PMID:DNA-dependent ATPase activity associated with phage P22 gene 12 protein. 615 40

The activities of 5'-nucleotidase (5'-ribonucleoside phosphohydrolase, EC 3.1.3.5); adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4); AMP deaminase (AMP aminohydrolase, EC 3.5.3.6), and ATP-(Mg2+)-ase (ATP phosphohydrolase, EC 3.6.1.3) were assayed in mitochondria of normal and regenerating rat liver 5'-Nucleotidase (5'Nase) and ATP-(Mg2+)-ase activities were compared with similar enzyme activities in the plasma membrane (PM) fraction, obtained from the same biological material. In the regenerating liver, 5'Nase for dTMP diminished its activity by 56% (24 h after partial hepatectomy) and 35 +/- 4% for all substrates in the PM fraction (48 h after operation). In mitochondria, 5'Nase for dTMP manifests sigmoidal substrate activity curve (in contrast with all substrates in the PM fraction and remaining substrates in mitochondria). In vivo 5-azacytidine (a) administered 1 h after partial hepatectomy, prevented changes of 5'Nase activity: (b) administered 24 or 48 h after partial hepatectomy, stabilized low 5'Nase activity (in mitochondria for dTMP, in the PM fraction for all substrates) and decreased ATP-(Mg2+)-ase activity by 51 and 31% in mitochondria and the PM fraction respectively.
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PMID:A distinctive activity of 5'-nucleotidase for dTMP in rat liver mitochondria. 615 75


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