Atpase

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Thank you for visiting nature. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser or turn off compatibility mode in Internet Explorer. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript. P-type ATPases use the energy from ATP hydrolysis to pump ions across the cell membrane against a concentration gradient. They form a large family of ubiquitous membrane proteins, and carry out many essential processes, such as generating the membrane potential or removing toxic ions from cells. P-type ATPases undergo large conformational changes in the ion-pumping cycle.

Atpase

ATPases EC 3. This dephosphorylation reaction releases energy , which the enzyme in most cases harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life. Some such enzymes are integral membrane proteins anchored within biological membranes , and move solutes across the membrane, typically against their concentration gradient. These are called transmembrane ATPases. Transmembrane ATPases import metabolites necessary for cell metabolism and export toxins, wastes, and solutes that can hinder cellular processes. ATPase is genetically conserved in animals; therefore, cardenolides which are toxic steroids produced by plants that act on ATPases, make general and effective animal toxins that act dose dependently. Besides exchangers, other categories of transmembrane ATPase include co-transporters and pumps however, some exchangers are also pumps. These are called electrogenic transporters and electroneutral transporters, respectively. The Walker motifs are a telltale protein sequence motif for nucleotide binding and hydrolysis. Beyond this broad function, the Walker motifs can be found in almost all natural ATPases, with the notable exception of tyrosine kinases. Protein design has been able to replicate the ATPase function weakly without using natural ATPase sequences or structures. Importantly, while all natural ATPases have some beta-sheet structure, the designed "Alternative ATPase" lacks beta sheet structure, demonstrating that this life-essential function is possible with sequences and structures not found in nature. Transmembrane ATPases make use of ATP's chemical potential energy by performing mechanical work: they transport solutes in the opposite direction of their thermodynamically preferred direction of movement—that is, from the side of the membrane with low concentration to the side with high concentration.

Aducci, P. Nature43—48

Thank you for visiting nature. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser or turn off compatibility mode in Internet Explorer. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript. F 1 F o ATP synthase interchanges phosphate transfer energy and proton motive force via a rotary catalysis mechanism.

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Atpase

ATPase adenosine triphosphatase. All rights reserved. Abbreviation for adenosine triphosphatase. An enzyme that catalyzes the formation of ATP from ADP, inorganic phosphate, and energy, found in mitochondria and chloroplasts; adenosine triphosphatase.

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Petrushanko et al used freshly isolated rat cerebellar granule cells to study oxygen sensitivity of the NKA function. Buch-Pedersen, M. Figure 3: P-type-ATPase structures and models. Boyer, P. Its name is due to short time attachment of inorganic phosphate at the aspartate residues at the time of activation. Modulation defect of sodium pump evidenced in diabetic patients by a microcalorimetric study. The ATP synthase - a splendid molecular machine. The NKA contains a binding site for cardiac glycosides, such as ouabain, digoxin, and digitoxin, which is highly conserved among species ranging from Drosophila to humans. Rabini and co-workers [ 48 ] observed that the structure of erythrocyte membranes, obtained from type-1 diabetic patients, showed a uncompetitive inhibition of the NKA, linked to the presence of conformational modifications of the protein. It could be a target for the development of anticancer drugs as it serves as a signal transducer, it is a player in cell adhesion and its aberrant expression and activity are implicated in the development and progression of different cancers. Recent X-ray structures and homology models of P-type pumps now provide a basis for understanding the molecular mechanism of ATP-driven ion transport. The new insight into the role of the distal lung epithelium in actively regulating lung fluid balance has important implications for the resolution of clinical pulmonary edema. Bukrinsky, J.

ATPases EC 3. This dephosphorylation reaction releases energy , which the enzyme in most cases harnesses to drive other chemical reactions that would not otherwise occur.

Blanco G, Mercer RW. The effects of cholesterol on enzyme activity are often also related to membrane fluidity [ 23 ]. The specific binding capacity for cardiac glycosides is utilized as a tool for NKA quantification with high accuracy and precision. Weidmann P, Ferrari P. The first X-ray structure of a P-type ATPase defines the four principal domains, and highlights a surprisingly long distance between the ion-translocation site in the membrane and the cytoplasmic phosphorylation site. Close banner Close. The sodium pump needs its beta subunit. Science , 69—77 Open in a separate window. The overall increase in ouabain-inhibitable NKA activity in vascular smooth muscle cells in response to insulin treatment suggests that, in the absence of insulin or in insulin-resistant states, NKA activity could decrease, resulting in increased vascular contractility and blood pressure. This dephosphorylation reaction releases energy , which the enzyme in most cases harnesses to drive other chemical reactions that would not otherwise occur. Moreover, activation of G protein-coupled receptors by agonists such as endothelin-1 elicits changes of NKA activity. Odermatt, A.