ATPasesA.G. Lee Elsevier, 17 груд. 1996 р. - 428 стор. Volume 5 of Biomembranes covers an important group of membrane proteins, the ATPases. The P-type ATPases couple the hydrolysis of ATP to the movement of ions across a membrane and are characterized by the formation of a phosphoyrlated intermediate. Included are the plasma membrane and muscle sarcoplasmic reticulum Ca2+ -ATPases, the (Na+ -K+) -ATPase, the gastric (H+ -K+) -ATPase, the plasma membrane H+ -ATPase of fungi and plants, the Mg2+ - transport ATPase, the Salmonella typhimurium, and the K+ -ATPase of Escherichia coli, KdpB. The other important classes of ATPase in eukaryotic systems are the vacuolar H+ -ATPases and the F0F1 ATP synthase, and, in bacteria, the anion-translocating ATPases, responsible for resistance to arsenicals and antimonials, and the (Na+ -Mg2+) -ATPase of Acholeplasma. Finally, eukaryotic systems contain a variety of ectonucleotidases important, for example, in hydrolysis of extracellular ATP released as a cotransmitter from cholinergic and adrenergic nerve terminals. Volume 5 of Biomembranes explores structure-function relationships for these mebrane-bound ATPases. |
Загальні терміни та фрази
Acta activity addition affinity alternative amino acid analysis apparent arsenate associated ATPase ATPase activity binding Biochem Biochemistry Biol Biophys Ca”-ATPase calcium cardiac catalytic cation cells characterization Chem cloning coli complex concentration conformation conserved contains cytoplasmic demonstrated dependent determined domain effect encoding enzyme et al evidence exchange expression extracellular Figure function gene glucose glycosylation H'-ATPase human hydrolysis identified important increase indicated inhibition inhibitors interaction involved isoforms isolated kinase kinetic labeling lipid located mechanism molecular muscle mutations Nelson nucleotide o-subunit observed peptide phosphorylation plasma membrane possible presence properties protein proton pump purified reaction region regulation release residues resistance role sarcoplasmic reticulum sector segment sequence showed shown side similar sodium pump specific step structure studies subunit suggested surface temperature transmembrane transport V-ATPase vesicles
Популярні уривки
Сторінка 361 - Grubmeyer, C., Cross, RL and Penefsky, HS (1982) Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase: Rate constants for elementary steps in catalysis at a single site.
Сторінка 419 - KUME. 1972. Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J. BioL Chem.