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

---

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

The influence of sulfhydryl reagents on ATPase systems of rabbit sceletal muscles nuclei was studied. It is found that p-ChMB at low concentration similarly inhibits both Mg2+- and Mg2+, Ca2+-ATPases. p-ChMB at higher concentrations inhibits completely Mg2+, Ca2+-ATPase, while Mg2+- ATPase--only by 60%. N-EM is lesser specific inhibitor of SH-groups, than p-ChMB. The degree of nuclear ATPases inhibition by N-EM is practically identical. Using inhibitory analysis, two hypes of skeletal muscles nuclei SH-groups are found: easily reacting with N-EM, and those reacting with N-EM at more high concentrations, which are essential for ATPase ATP-hydrolysing activity. ATP defends Mg2+, Ca2+-ATPase, but not the Mg2+-ATPase from N-EM inhibitory action. Cysteine completely eliminates the inhibitory effect of p-ChMB on Mg2+-ATPase but only 40% on MG2+, Ca2+-ATPase. Mg2+, Ca2+-ATPase of nuclei is more sensitive to the sulfhydryl venoms action than Mg2+-ATPase.
...
PMID:[Effect of SH-reagents on ATPase systems of rabbit skeletal muscle nuclei]. 14 67

The 2',3'-dialdehyde ATP analog (oATP) was synthesized and its ability to activate the Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum via the adenosine-nucleotide-binding site was investigated. After reduction by sodium borohydride, oATP binds covalently to the catalytic adenosine-nucleotide-binding site of the enzyme, resulting in 85% loss of acetyl-phosphate-driven Ca2+ uptake and ATP-hydrolysing ability. In the absence of a reducing agent, oATP serves as a substrate for the Ca(2+)-ATPase, as indicated by Pi formation (hydrolysis) and Ca(2+)-uptake ability. oATP binding to the intact light sarcoplasmic reticulum is observed in the absence and presence of the competitive adenosine nucleotide inhibitor, fluorescein isothiocyanate with apparent affinity constants of 1.2 mM and 2.2 mM, respectively. Autoradiography of tryptic fragments from partially purified Ca(2+)-ATPase labeled with [alpha-32P]oATP or [gamma-32P]oATP locates the covalent binding site to the A1 fragment, even in the fluorescein-isothiocyanate-labeled pump protein. With high probability, a lysine residue in the tryptic A1 fragment is labeled by the ribose-modified ATP analog close to the phosphorylation site at Asp351.
...
PMID:2',3'-Dialdehyde ATP analog labels the Ca(2+)-ATPase of sarcoplasmic reticulum via the catalytic adenosine-nucleotide-binding site. 153 53

We investigated the interaction of triethyllead with ATP-coupled cellular enzymatic activities and the role of GSH to reverse the observed inhibition of these enzymes. Triethyllead inhibited the membrane bound Na+-K+-ATPase from HeLa cells (IC50 12 microM) and the ATP-hydrolysing activity of the mitochondrial F0-F1-ATPase complex (IC50 17 microM). Addition of 1 mM GSH reversed both enzyme activities totally, whereas lower GSH concentrations showed a less pronounced effect. Surprisingly, in freshly isolated rat liver mitochondria the ATP-synthesizing activity was also inhibited by triethyllead (IC50 16 microM), in spite of a measured high intramitochondrial GSH concentration (up to 10 mM). Further experiments in isolated submitochondrial particles revealed that ATP-synthesis and ATP-hydrolysis were inhibited by triethyllead with similar IC50 values, and both activities could be protected in vitro from the organolead compound in the presence of 1 mM GSH. Thus in all activities tested in vitro a high excess of GSH over triethyllead (greater than or equal to 25-fold) is necessary to restore the inhibited enzymes. The intramitochondrial triethyllead concentration was further determined after incubation of intact mitochondria with 10 microM of the organolead compound. The organolead concentration measured was as high as 600 microM. This means that in intact mitochondria there exists only a ca. 16-fold excess of GSH, which has been shown to be insufficient to protect ATP-synthesizing and ATP-hydrolyzing activities of the F0-F1-ATPase from triethyllead in vitro. We concluded that in intact mitochondria the F0-F1-ATPase complex is inhibited by triethyllead due to its accumulation in the matrix.
...
PMID:Inhibition of cellular activities by triethyllead. Role of glutathione and accumulation of triethyllead in vitro. 255 37

The proton-translocating adenosine triphosphatase (ATPase) of bovine chromaffin granules contains up to five different polypeptides. Its activity is inhibited by N-ethylmaleimide, and ATP protects the enzyme from inhibition. After treatment of membranes with N-[2-3H]ethylmaleimide, only one polypeptide is strongly radiolabelled: this is the largest (70 kDa) subunit of the proton-translocating ATPase. This subunit therefore contains the ATP-hydrolysing site. Two-dimensional electrophoresis reveals heterogeneity in this polypeptide.
...
PMID:Proton-translocating adenosine triphosphatase of chromaffin-granule membranes. The active site is in the largest (70 kDa) subunit. 287 37

Ca2+-uptake activities of the sarcoplasmic reticulum (SR) were determined with a Ca2+-sensitive electrode in homogenates from fast- and slow-twitch muscles from both normal and dystrophic mice (C57BL/6J strain) of different ages. Immunochemical quantification of tissue Ca2+-ATPase content allowed determination of the specific Ca2+-transport activity of the enzyme. In 3-week-old mice of the dystrophic strain specific Ca2+ transport was already significantly lower than in the normal strain. It progressively decreased with maturation and reached only 40-50% and 30-50% of the normal values in fast- and slow-twitch muscles of adult dystrophic animals, respectively. Tissue contents of calsequestrin were reduced in both types of muscle leading to an increased Ca2+-ATPase to calsequestrin protein ratio. Equal amounts of the Ca2+-ATPase protein (detected by Coomassie blue staining of polyacrylamide gels) were present in SR vesicles isolated by Ca2+-oxalate loading from adult normal and dystrophic fast-twitch muscles. However, the specific ATP-hydrolysing activity of the enzyme was approximately 50% lower in dystrophic than in normal SR. The reduced ATP-hydrolysing activity was correlated with decreased Ca2+-transport activity, phosphoprotein formation and fluorescein isothiocyanate labeling as determined in total microsomal and heavy SR fractions. Although the Ca2+ and ATP affinities of the enzyme were unaltered, its ATPase activity was reduced at all levels of ATP in the dystrophic SR. Taken together, these findings point to a markedly impaired function of the SR and an increase in the population of inactive SR Ca2+-ATPase molecules in murine muscular dystrophy.
...
PMID:Postnatal development of Ca2+-sequestration by the sarcoplasmic reticulum of fast and slow muscles in normal and dystrophic mice. 296 44

The ouabain-sensitive ATP-hydrolysing activity, representing the Na+/K+ ATPase capacity, of isolated membranes and whole cells during and after hyperthermia treatments was investigated. In isolated membranes no heat damage after treatments up to 46 degrees C during 45 min or up to 6 h at 44 degrees C could be detected. The ATP hydrolysing activity of Na+/K+ ATPase seems not to be impaired by direct heat attack in the range of commonly used hyperthermic temperatures (39-46 degrees C). Heat effects on the ATP hydrolysing activity of Na+/K+ ATPase of whole mouse fibroblasts could only be detected after heat doses (greater than 40 min at 44 degrees C) necessary to yield over 99 per cent dead cells. Potassium influx, measured with 86RB+ as the K+ tracer, was initially enhanced during incubation at 44 degrees C proportionally with the enhancement of the ATP-hydrolysing activity after raising the temperature. Replacement of non-lethally (10 min at 44 degrees C) and lethally (40 min at 44 degrees C) treated mouse fibroblasts to 37 degrees C showed complete reversibility of the enhanced activity at 44 degrees C to the control level at 37 degrees C. For comparison, the ATP-hydrolysing activity of Na+/K+ ATPase of HeLa S3 cells growing as monolayer was also tested. The activity after heat treatments up to 60 min at 44 degrees C was also found to be unchanged in these experiments. No indication of irreversible damage to the ATP-hydrolysing capacity of mouse fibroblasts and HeLa S3 cells, or K+ pumping activity of mouse fibroblasts by heat treatments up to 40 min at 44 degrees C was found.
...
PMID:Na+/K+ ATPase activity in mouse lung fibroblasts and HeLa S3 cells during and after hyperthermia. 301 21

An alkylating ATP analogue, gamma-[4-(N-2-chlorethyl-N-methylamino)]benzylamide ATP (C1RATP), covalently binds to the catalytic alpha-subunit of Na+, K+-ATPase yielding a product resistant to hydrolysis by the enzyme and inhibiting the ATP-hydrolysing activity. The Na+-form of the membrane-bound Na+, K+-ATPase modified with C1RATP was hydrolysed by pepsin under conditions providing maximum stability of the modification product (4 degrees C, pH 1.5). The modified peptide was isolated by HPLC and its amino acid sequence was found to involve residues 706-713 of the alpha-subunit polypeptide chain. This fragment located near the gamma-phosphate of ATP is a component of the active site. It is highly homologous with corresponding regions of the catalytic subunits of all the known E1-E2 ATPases. In the Na+-(or E1-)enzyme form Asp-710 is the target of modification. Evidently E1- and E2-enzymes have different targets in C1RATP modification, i.e. the polypeptide chain regions near the ATP gamma-phosphate in the enzyme active site differ somewhat in their conformations.
...
PMID:Affinity modification of E1-form of Na+, K+-ATPase revealed Asp-710 in the catalytic site. 303 72

An ATP-hydrolysing activity on the external surface of intact synaptosomes from chicken forebrain has been investigated. The observed ATPase activity was not due to leakage of the intracellular ATPase activities, of artefacts resulting from breakage of the nerve endings during the incubation and isolation periods, or to possible contamination by other subcellular particles. Disruption of the synaptosomes resulted in an approximately 2.5-fold increase of the basal, Mg2+-dependent ATPase activity, suggesting that the plasma membrane was acting as permeability barrier to the substrate. ATP hydrolysis was maximal (0.8 mumol Pi/min/mg protein) at pH 8.2 in a medium containing either Mg2+ or Ca2+ ions. Ouabain (0.2 mM) and oligomycin (2 micrograms/mg protein) had no appreciable effect on this ATPase activity. Kinetic studies of the enzyme revealed an apparent Km value of ATP of approximately 4 x 10(-5) M. These data are consistent with the view that the observed ATP hydrolysis was being catalysed by an ectoenzyme, i.e., an enzyme in the plasma membrane of the nerve endings with its active site facing the external medium. The rapid hydrolysis of the released ATP is a suspected function for this ecto-ATPase.
...
PMID:Adenosine triphosphatase activity at the external surface of chicken brain synaptosomes. 612 88

Very little is currently known about the ouabain-insensitive ATPase activity of the liver plasma membrane; we have therefore characterized it in plasma membranes from rat liver prepared using two different isolation techniques. Greater than 85% of ATPase activity in both preparations was ouabain-insensitive. Based on the effects of multiple inhibitors, including dicyclohexylcarbodiimide (DCCD), N-ethylmaleimide (NEM), vanadate, and oligomycin, the ouabain-insensitive ATPase activity of rat liver plasma membranes consists of a family of ATP-hydrolysing enzymes. Ouabain-insensitive ATPase activity was stimulated by HCO3-in both plasma membranes (13%) and mitochondria (69%) over the range of 7.5 to 9.0, and HCO3--stimulation was similarly inhibited by oligomycin in both preparations. A fraction of the ouabain-insensitive ATPase of liver plasma membranes is inhibited by DCCD and is resistent to inhibition by oligomycin; these characteristics are similar to those of the non-mitochondrial H+-ATPases recently described in lysosomes, endosomes, clathrin-coated vesicles, and Golgi from liver and other cell types.
...
PMID:Characterization of the ouabain-insensitive ATPase activity of rat liver plasma membranes. 620 61

The oleB gene of Streptomyces antibioticus, oleandomycin producer, encodes an ABC transporter containing two putative ATP-binding domains and is involved in oleandomycin resistance and secretion in this organism. We have overexpressed in Escherichia coli the N-terminal nucleotide-binding domain of OleB (OleB') as a fusion protein and purified the fusion protein by affinity chromatography. The fusion protein showed ATPase activity dependent on the presence of Mg2+ ions. ATPase activity was resistant to specific inhibitors of P-, F-, and V-type ATPase whereas sodium azide and 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-C1) were strong inhibitors. The change of Lys71, located within the Walker A motif of the OleB' protein, to Gln or Glu caused a loss of ATPase activity, whereas changing to Gly did not impair the activity. The results suggest that the intrinsic ATPase activity of purified fusion protein can be clearly distinguished from other ATP-hydrolysing enzymes, including ion-translocating ATPases or ABC-traffic ATPases, both on the basis of inhibition by different agents and since it hydrolyzes ATP without interacting with a hydrophobic membrane component.
...
PMID:Characterization of the ATPase activity of the N-terminal nucleotide binding domain of an ABC transporter involved in oleandomycin secretion by Streptomyces antibioticus. 876 17


1 2 Next >>

---