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)

The distribution of enzymes, viz., alkaline phosphatase, acid phosphatase, adenosine monophosphatase and adenosine triphosphatase was studied by histochemical methods in the accessory respiratory organs of two fresh-water fishes (Clarius batrachus and Heteropneustes fossilis). Enzymes have been used as markers to differentiate between functional and non-functional cells of the dendritic organ of Clarius and of the air chamber of Heteropneustes. The variations in the enzyme activities have been correlated with the functional capacity of each respiratory organ. It is attempted to understand the physiological role of these enzymes in the process of aerial breathing.
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PMID:Phosphatases in the accessory respiratory organs of two fresh-water fishes. 20 22

Chronic ethanol administration to cats increased specific [3H]ouabain binding by 63% in cerebral cortex, 47% in cerebellum, 84% in amygdala, and 100% in hippocampus when the binding assays were performed in the presence of 160 nM [3H]ouabain. There was no significant change in specific [3H]ouabain binding in hypothalamus, thalamus, corpus striatum, and brain stem following chronic ethanol ingestion. Scatchard analysis revealed that enhancement of specific [3H]ouabain binding following chronic ethanol treatment in some areas of cat brain is primarily due to changes in densities of ouabain binding sites. Since ouabain is a specific inhibitor of (Na+ + K+)-ATPase the present observations suggest that the molecular mechanism for the enhancement of (Na+ + K+)-ATPase activity after chronic ethanol ingestion may be due to increased net rate of synthesis of (Na+ + K+)-ATPase molecules or exposure of non-functional enzyme system following conformational change of plasma membrane.
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PMID:Effect of chronic ethanol treatment on specific [3H]ouabain binding to (Na+ + K+)-ATPase in different areas of cat brain. 22 78

We have introduced multiple cytosine-to-uracil mutations in the rho-dependent transcription terminator trp t' and have characterized a subset of the resulting mutant derivatives in vitro for termination efficiency, affinity for rho, and stimulation of rho-ATPase activity. No specific cytosine residue appears to be required for termination, and at least 13 of the 28 cytosine residues in the 104 nucleotide trp t' region can be mutated with little effect on termination efficiency. One derivative with 11 mutations is significantly less efficient than other derivatives with a similar number of mutations, implying that the pattern of alterations, as well as the number, can affect termination efficiency. Derivatives with 20 and 28 cytosines mutated are non-functional in termination, consistent with the idea that cytosines are required for rho-dependent termination. Our results are inconsistent, however, with the hypothesis that the termination efficiency is directly related to the cytosine/guanine ratio in the nascent transcript. The results support the idea that neither RNA binding affinity nor ATPase activation per se are accurate predictors of rho-dependent termination efficiency.
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PMID:Effects of decreased cytosine content on rho interaction with the rho-dependent terminator trp t' in Escherichia coli. 138 63

This work concerns a biochemical genetic study of subunit 9 of the mitochondrial ATPase complex of Saccharomyces cerevisiae. Subunit 9, encoded by the mitochondrial oli1 gene, contains a hydrophilic loop connecting two transmembrane stems. In one particular oli1 mit- mutant 2422, the substitution of a positively charged amino acid in this loop (Arg39----Met) renders the ATPase complex non-functional. A series of 20 revertants, selected for their ability to grow on nonfermentable substrates, has been isolated from mutant 2422. The results of DNA sequence analysis of the oli1 gene in each revertant have led to the recognition of three groups of revertants. Class I revertants have undergone a same-site reversion event: the mutant Met39 is replaced either by arginine (as in wild-type) or lysine. Class II revertants maintain the mutant Met39 residue, but have undergone a second-site reversion event (Asn35----Lys). Two revertants showing an oligomycin-resistant phenotype carry this same second-site reversion in the loop region together with a further amino acid substitution in either of the two membrane-spanning segments of subunit 9 (either Gly23----Ser or Leu53----Phe). Class III revertants contain subunit 9 with the original mutant 2422 sequence, and additionally carry a recessive nuclear suppressor, demonstrated to represent a single gene. The results on the revertants in classes I and II indicate that there is a strict requirement for a positively charged residue in the hydrophilic loop close to the boundary of the lipid bilayer. The precise location of this positive charge is less stringent; in functional ATPase complexes it can be found at either residue 39 or 35. This charged residue is possibly required to interact with some other component of the mitochondrial ATPase complex. These findings, together with hydropathy plots of subunit 9 polypeptides from normal, mutant and revertant strains, led to the conclusion that the hydrophilic loop in normal subunit 9 extends further than previously suggested, with the boundary of the N-terminal membrane-embedded stem lying at residue 34. The possibility is raised that the observed suppression of the 2422 mutant phenotype in class III revertants is manifested through an accommodating change in a nuclear-encoded subunit of the ATPase complex.
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PMID:Amino acid substitutions in subunit 9 of the mitochondrial ATPase complex of Saccharomyces cerevisiae. Sequence analysis of a series of revertants of an oli1 mit- mutant carrying an amino acid substitution in the hydrophilic loop of subunit 9. 295 97

The effect of ethanol and other low molecular weight alcohols having an anaesthetic action, on the activity of Ca-ATPase (EC 3.6.1.38) as well as on the Ca2+ uptake and efflux and the functional efficiency of Ca-pump in rabbit skeletal muscle sarcoplasmic reticulum membranes was studied. It was found that some alcohols, especially when taken at low concentrations, specifically stimulate the activity of the Ca-pump and Ca-ATPase. The concentration (C) of the alcohol at which the maximum value of the Ca/ATP ratio is achieved, is well correlated with the value of the partition coefficient (P) for this alcohol in a two-phase water/octanol system. As the concentration of an alcohol rises, it primarily affects the release of Ca2+, but the Ca-pump still functions well and is able to compensate for the Ca2+ leakage up to a certain moment, after which the phospholipid bilayer structure changes crucially, and is beginning the denaturation of Ca-ATPase. Finally the increase in the concentration of either of the alcohols results in a complete loss of the Ca-ATPase activity. The specific effect of alcohols cannot be explained in terms of an unitary mechanism based on fluidity changes in the membrane. It is assumed that at low concentrations certain alcohols (or groups of related alcohols) are able to promote the specific transition of membrane proteins into the active state, whereas at higher concentrations all alcohols provide for the non-functional state of the proteins.
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PMID:[Dual effect of ethanol and other aliphatic alcohols on the effectiveness of the Ca-pump and Ca-ATPase activity of the sarcoplasmic reticulum of skeletal muscles]. 296 44

The effect of 10 low molecular mass alkanols on the activity of Ca-ATPase (EC 3.6.1.38), Ca uptake and Ca efflux as well as the functional efficiency of the Ca pump in the fragmented sarcoplasmic reticulum of rabbit skeletal muscles has been studied. Some alkanols, especially when taken at low concentration, have been found to stimulate the activity of the Ca pump and Ca-ATPase, namely tert-butanol, isopropanol and ethanol (from the group of hydrophilic alkanols), and pentanol, isopentanol and hexanol (from the more hydrophobic alkanols). Methanol (from the first group) and isobutanol, butanol and propanol (from the second) do not stimulate the Ca pump compared with the control. The specific effect of different alkanols cannot be explained in terms of a unitary mechanism based on 'fluidity' changes of the membrane. It is assumed that, at low concentrations, certain alkanols (or groups of related alkanols) are able to promote the specific transition of membrane proteins into the active state, whereas at higher concentrations all alkanols provide for the non-functional state of the proteins.
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PMID:Short-chain alkanols and the functional efficiency of the Ca pump in the sarcoplasmic reticulum of rabbit skeletal muscles. 296 86

Expression studies of Propionigenium modestum ATPase genes in various combinations with Escherichia coli ATPase genes were performed in the unc deletion mutant strain E. coli DK8. Plasmids containing the whole unc operon from P. modestum were unable to complement the E. coli unc deletion mutant. Although all ATPase subunits were expressed from the plasmids, there was no detectable ATP hydrolysing activity, indicating that the F1 part was not functional. Transformants expressing an E. coli F1-P. modestum F0 hybrid exhibited considerable ATPase activities. Binding of the F1 part to the membrane was very weak, however, and the coupling between ATP hydrolysis and Na+ transport was impaired. After combining the genes for E. coli ATPase subunits alpha, beta, gamma, delta and epsilon and the hydrophilic part of subunit b with P. modestum ATPase subunits a and c and the hydrophobic part of subunit b on a plasmid, a non-functional hybrid ATPase was expressed in E. coli. The ATPase was only loosely bound to the membrane, from which it was solubilized with Triton X-100 and purified. Subunit b and a proteolytic degradation product were the only F0 subunits detectable in the purified enzyme. A stable F0 complex is thus not formed with the hybrid b subunit. The absence of a functional F0 complex was in accord with proton-conduction measurements with bacterial vesicles. The only functional Na(+)-translocating ATPase expressed in E. coli thus far consists of E. coli subunits alpha, beta, gamma and epsilon, and P. modestum subunits delta, a, b and c [Kaim, G. & Dimroth, P. (1993) Eur. J. Biochem. 218, 937-944]. During the cloning conducted in our present study, errors in the sequence entry into the EMBL data bank (accession no. X58461) for the P. modestum ATPase alpha and beta subunits became evident, which are corrected in this paper.
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PMID:In vivo synthesis of ATPase complexes of Propionigenium modestum and Escherichia coli and analysis of their function. 755 12

A biochemical investigation was carried out on the relative presence of some enzymes of the Krebs cycle and of the associated energy metabolism in various fractions (namely, cyst wall, cyst fluid and zoites) of sarcocysts of Sarcocystis fusiformis from the oesophageal muscles of naturally infected Indian water buffalo (Bubalus bubalis). Except for malate dehydrogenase, the activities of aconitase, isocitrate dehydrogenase, succinate dehydrogenase and fumarase were beyond detectable limits, pointing to a non-functional Krebs cycle in the cysts of this parasite. The activities of adenosine triphosphatase and cytochromes were lowest in cyst fluid and were maximally depicted by cyst wall and zoites.
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PMID:Sarcocystis fusiformis: some Krebs cycle enzymes in various fractions of sarcocysts of buffalo (Bubalus bubalis). 773 35

The baculovirus expression system is suitable for functional expression of gastric H+,K(+)-ATPase. Expression of functional H+,K(+)-ATPase in Sf9 cells is accompanied by synthesis of large amounts of non-functional subunits. When H+,K(+)-ATPase is synthesised in the presence of 150-250 mM ethanol in the culture medium, two to threefold higher levels of functional H+,K(+)-ATPase are produced due to the formation of more functional subunits rather than to an increase of subunits per se. The catalytical properties of the ethanol-produced H+,K(+)-ATPase are indistinguishable from control preparations. The mechanism by which ethanol stimulates the formation of functional H+,K(+)-ATPase probably involves a direct effect on the physical properties of Sf9 membranes. In addition there also might be an indirect effect through ethanol inducible stress proteins acting as molecular chaperones.
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PMID:Ethanol stimulates expression of functional H+,K(+)-ATPase in SF9 cells. 776 63

The germinating asexual spores (conidia) of Neurospora crassa were employed to study steps in the accumulation of transcripts of groups of mitochondrial genes, including those for peptide subunits of cytochrome c oxidase (CO), ATPase (ATP), and apocytochrome b (COB). Physically clustered groups of genes were expressed as cohorts: transcripts of the ATP8-ATP6-mtATP9-CO2 genes were almost undetectable in the dormant spores, and they accumulated rapidly as a group immediately after spore activation. Transcripts of COB and the adjacent CO1 were abundant in the dormant spores, and the dormant and germinating spores contained size forms of the COB transcripts that were not evident in vegetative cells. Polyribosomes were prepared from mitochondrial lysates, and the polyribosomal RNA was probed to identify the mRNAs of specific genes; in several instances polycistronic mRNAs were present in the polyribosomes as were the smaller end-products of the inferred transcript processing pathways. The expression of the physically dispersed genes for subunit peptides of cytochrome c oxidase appears to be regulated to the level of translation; these transcripts are accumulated in the total mitochondrial RNA with sharply different kinetics, but they appeared in the polyribosomes uniformly, their appearance correlating with the uniform synthesis of the subunit peptides. Transcripts for a previously reported non-functional mitochondrial gene, homologous to the functional nuclear gene for ATPase subunit 9, were found in the germinating spores, but were not detected in vegetative cells. These mtATP9 transcripts were also present in the polyribosomes and were apparently translated into a protein in vivo whose synthesis was insensitive to cycloheximide and detectable with an anti-ATP9 subunit antibody. Transcripts for two nuclear genes for mitochondrially localized proteins, ATP9 and CO5, were accumulated in unison and especially rapidly during spore germination.
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PMID:Expression of mitochondrial genes in the germinating conidia of Neurospora crassa. 828 26


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