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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Apyrase activity has been found in tissue of all investigated plant species. Seedlings soluble fractions accounted for 45-75% of the cell apyrase activity, whereas the apyrases isolated from microsomes accounted for 0.2-7% of the total homogenate activity. The ratio of the rate of ATP hydrolysis to the rate of ADP hydrolysis, Ksh, divides the apyrases into two groups: of Ksh > 1 (enzymes from most of monocot plants and bovine tissues) and of Ksh < 1 (enzymes from dicot plants). Triflupromazine strongly decreased the activity of wheat and bovine apyrases (first group) and does not inhibit the activity of the enzyme from potato (second group). Analysed apyrases reveal a significant antigenic diversity. Antibodies developed against soluble potato apyrase have no affinity to apyrase from microsomes of wheat seedlings. Immunological analysis confirmed that ATPase and ADPase activities of potato apyrase were associated with one protein. Apyrases, including animal ones, are insensitive to ATPases inhibitors and reagents of SH groups, whereas sodium deoxycholate inhibits all of the studied enzymes. NaF decreases activity plant enzymes, whereas erythrosine B and NaN3 only decreases bovine apyrases.
Comp Biochem Physiol B Biochem Mol Biol 1996 Mar
PMID:Comparative studies on animal and plant apyrases (ATP diphosphohydrolase EC 3.6.1.5) with application of immunological techniques and various ATPase inhibitors. 882 8

Extracellular nucleotides interact with specific receptors on the cell surface and are locally metabolized by ecto-nucleotidases. Biochemical characterization of the ATPase and ADPase activities detected in rat heart sarcolemma, under conditions where mitochondrial ATPase and adenylate kinase were blocked, supports our proposal that both activities correspond to a single enzyme, known as ATP-diphosphohydrolase or apyrase. The physiological function of this enzyme could be dephosphorylation of the nucleotides present in the interstitial heart compartment acting together with 5'-nucleotidase. Both hydrolytic activities have similarities in: sarcolemma localization, bivalent metal ion dependence, optimum pH, effect of several amino acid residue modifiers, competitive inhibition of nucleotide analogs, and broad nucleoside di-and triphosphate specificity. The ATPase activity could not be separated from the ADPase either through isoelectrofocusing or electrophoresis under acid conditions.
Biochem Mol Biol Int 1996 Aug
PMID:ATP-diphosphophydrolase activity in rat heart tissue. 886 7

An apyrase and an alpha-glucosidase were detected in the salivary glands extracts of adult Aedes albopictus. The apyrase is a 61,000 Da secreted protein that hydrolyses ATP and ADP. This protein is synthe-sized in adults and is preferentially accumulated in the distal lateral lobes of the female salivary glands. The alpha-glucosidase is a secreted 67,000 Da protein. This enzyme is synthesized during adult life and accumulated in the proximal-lateral lobes of both males and females. The results are discussed and compared with data previously obtained with Aedes aegypti salivary glands.
Comp Biochem Physiol B Biochem Mol Biol 1996 Apr
PMID:Apyrase and alpha-glucosidase in the salivary glands of Aedes albopictus. 892 36

In the present report we demonstrate the in vitro effects of free radicals on an ecto-ATP diphosphohydrolase activity (apyrase, EC 3.6.1.5) from rat blood platelets. Rat blood platelets were exposed to an oxidant-generating system (H2O2/Fe2+/ascorbate) and the ATP diphosphohydrolase activity was inhibited. The enzyme inhibition was prevented by glutathione (GSH) and cysteine but not by trolox as a vitamin E analogue. The TBARS (thiobarbituric acid reactive substances) assay and the determination of sulphydryl groups indicate that the inhibition of the enzyme activity in resting platelets is not related to lipid peroxidation or to oxidation of sulphydryl residues. These results demonstrate the susceptibility of ATP diphosphohydrolase activity from platelets to free radicals and suggest that amino acid residues which are essential for the enzyme function are probably modified.
Biochem Mol Biol Int 1997 Jan
PMID:Free radical-induced inhibition of ATP diphosphohydrolase activity (EC 3.6.1.5) from rat blood platelets. 904 45

In the present report we describe an ATP diphosphohydrolase (apyrase EC 3.6.1.5) in rat cardiac sarcolemma. It is Ca2+ dependent and is insensitive to ouabain, orthovanadate, N-ethylmaleimide (NEM), lanthanum, and oligomycin that are classical ATPase inhibitors. Sodium azide that is a mitochondrial inhibitor at low concentrations, did not affect the enzyme activity at 5.0 mM or below. In contrast, at high concentrations (> 10 mM) sodium azide inhibited the enzyme. Levamisole, a specific inhibitor of alkaline phosphatase and P1, P5-di(adenosine 5'-)pentaphosphate (Ap5A), a specific inhibitor of adenylate kinase did not inhibit the enzyme. Mercury chloride showed a parallel inhibition of the hydrolysis of both substrates of apyrase. Similar inhibition profiles are powerful evidence for a common catalytic site for the hydrolysis of both substrates. The enzyme has an optimum pH range of 7.5-8.0 and catalyzes the hydrolysis of triphospho- and diphosphonucleosides other than ATP or ADP. The apparent Km (Michaelis constant) and Vmax (maximal velocity) are 62.1 +/- 5.2 microM and 1255.7 +/- 178 micromol inorganic phosphate liberated/min/mg with ATP and 59.4 +/- 4.3 microM and 269.2 +/- 39 micromol inorganic phosphate liberated/min/mg with ADP. Enzyme markers indicated that this apyrase is associated with the plasma membrane. A deposition of lead phosphate granules on the outer surface of the sarcolemmal vesicles was observed by electron microscopy in the presence of either ATP or ADP as substrate. It is suggested that the ATP diphosphohydrolase could regulate the concentration of extracellular adenosine, and thus is important in the control of vascular tone and coronary flow.
Mol Cell Biochem 1997 May
PMID:Characterization and localization of an ATP diphosphohydrolase activity (EC 3.6.1.5) in sarcolemmal membrane from rat heart. 914 25

Periplasmic 5'-nucleotidase from Escherichia coli, in addition to the monophosphoesterase activity has a diphosphohydrolase activity, acting on nucleoside di- and triphosphates. We proposed that the monophosphoesterase and diphosphohydrolase activities have their own active site. This proposal is based on the different types of bonds being broken. Chemical modification with selective group reagents did not show differences in the essentiality of some residues, like histidyl, carboxyl and arginyl groups, of these two hydrolytic activities. While kinetic approaches employing the competition plot and unidirectional substrate inhibition point to that diphosphohydrolase activity (ATPase-ADPase) do not share the same active site with monophosphoesterase activity. Western blotting developed with polyclonal anti-placental apyrase antibody revealed a single protein in the periplasmic fraction of 66.5 kDa similar to the Mr of the purified enzyme by isoelectrofocusing.
Comp Biochem Physiol B Biochem Mol Biol 1997 May
PMID:Kinetic characteristics of nucleoside mono-, di- and triphosphatase activities of the periplasmic 5'-nucleotidase of Escherichia coli. 918 21

A rat brain cDNA coding for ecto-(Ca,Mg)-apyrase activity was isolated using human CD39 cDNA and functionally expressed in COS-7 cells. The gene codes for a protein with high similarity to human (75% identity) and murine (90% identity) CD39. It is expressed in primary neurons and astrocytes in cell culture as well as in kidney, liver, muscle and spleen. Southern analysis of the mouse genome suggests that there may be a single copy of the ecto-apyrase gene. Interestingly, the human CD39 gene cytologically co-localizes with the susceptibility gene involved in human partial epilepsy with audiogenic symptoms; such a coincidence is consistent with reports on the deficiency of ecto-apyrase activity in the brains of humans with temporal lobe epilepsy and in those of mice with audiogenic seizures.
Brain Res Mol Brain Res 1997 Jul
PMID:Characterization of brain ecto-apyrase: evidence for only one ecto-apyrase (CD39) gene. 922 28

Ectoenzymic activities capable of hydrolyzing ATP sequentially to adenosine are present on equine epidydimal spermatozoa membranes. Kinetic parameters for ATPase, ADPase and 5'-nucleotidase were obtained by analysis of progress reactions curve when ATP, ADP and AMP were supplied as initial substrates. These values are not different from those found when the substrates were supplied from the preceding reactions. Feed-forward inhibition on 5'-nucleotidase by ATP/ADP was taken into account to fit simulated data to the experimental results. None of the substrates supplied by the preceding reactions showed a preferential delivery to ADPase and/or 5'-nucleotidase. We therefore conclude that the model that fits the equine spermatozoa is that already proposed for pig aortic endothelial cells.
Comp Biochem Physiol B Biochem Mol Biol 1997 Aug
PMID:Hydrolysis of extracellular adenine nucleotides by equine epidydimal spermatozoa. 929 97

We have investigated the effect of cross-linking on the enzymatic activity and oligomer formation of the chicken stomach ecto-apyrase. Cross-linking with the hydrophobic, lysine-specific dithiobis(succinimidylpropionate) (DSP) caused equal inhibition of ATPase and ADPase activity in both the membrane-bound and detergent-solubilized ecto-apyrase. The inhibitory effect of cross-linking was reversed upon the addition of the reductant dithiothreitol. Western blots of aliquots of the cross-linked samples show decreased amounts of the monomeric 80 kDa ecto-apyrase and the appearance of a 160 kDa dimer under conditions inducing enzyme inhibition. Therefore, the chicken stomach ecto-apyrase, like the chicken gizzard ecto-ATPase, is likely a homodimer in vivo. Unlike the related gizzard ecto-ATPase, however, the native stomach ecto-apyrase is not stimulated, but rather inhibited by cross-linking, presumably due to different quaternary structural stability of the two enzymes.
Biochem Mol Biol Int 1998 Mar
PMID:Cross-linking induces homodimer formation and inhibits enzymatic activity of chicken stomach ecto-apyrase. 955 6

Nucleoside triphosphate hydrolase is an abundant protein secreted by the obligate protozoan parasite Toxoplasma gondii. The protein has apyrase activity, degrading ATP to the di- and mono-phosphate forms. Because T. gondii is incapable of de novo synthesis of purines, it is postulated that NTPase may be used by the parasite to salvage purines from the host cell for survival and replication. To elucidate the molecular mechanisms of NTP gene expression, we isolated from the virulent RH strain of T. gondii the putative promoter region of three tandemly repeated NTP genes (NTP1, 2, 3). Using deletion constructs linked to the chloramphenicol acetyl transferase (CAT) reporter gene, we defined an active promoter within the first 220 bp. Sequence analysis of this region reveals the lack of a TATA box, but the promoter region is associated with a sequence which resembles an initiator element (Inr) in the NTP1 and NTP3 genes. This sequence which is similar to other Inrs known to regulate the expression of a wide variety of RNA polymerase II genes, is required for NTP expression. The NTP3 promoter contains sufficient information for developmentally regulated expression of CAT activity when the actively replicating stage tachyzoite differentiates into the dormant bradyzoite form.
Mol Biochem Parasitol 1998 May 01
PMID:Upstream elements required for expression of nucleoside triphosphate hydrolase genes of Toxoplasma gondii. 965 28


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