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)

Two separate genes encode fast-twitch and slow-twitch/cardiac muscle forms of the Ca2+ ATPase of sarcoplasmic reticulum. Full length Ca2+ ATPase clones have been isolated from adult rabbit fast-twitch, slow-twitch, and cardiac muscles. Segments of these clones containing unique sequences have been used as probes to study developmental changes in Ca2+ ATPase transcripts. The fast-twitch Ca2+ ATPase transcript undergoes developmentally regulated alternative splicing in which a penultimate 42-base pair exon is retained in the adult transcript but is excised in the neonatal transcript. This additional exon shifts the exon encoding the neonatal carboxyl-terminal sequence, -Asp-Pro-Glu-Asp-Glu-Arg-Arg-Lys (Brandl, C. J., Green, N. M., Korczak, B., and MacLennan, D. H. (1986) Cell 44, 597-607) into a nontranslated region and results in the expression of an adult isoform with a carboxyl-terminal -Gly. The neonatal form of the fast-twitch Ca2+ ATPase represents 72% of the fast-twitch Ca2+ ATPase transcripts just prior to birth but only 17% by 14 days of age and 4% in adult fast-twitch muscle. Adult slow-twitch, adult cardiac, and neonatal skeletal muscles express an identical Ca2+ATPase mRNA transcript which is distinct from either of the fast-twitch forms. The slow-twitch/cardiac Ca2+ ATPase is the predominant form expressed in late fetal and early neonatal rabbit skeletal muscle, but this form is lost as the skeletal muscle differentiates into a fast-twitch state. Three or more alternative polyadenylation signals exist for this mRNA in all tissues with the most 3' signal predominating.
...
PMID:Adult forms of the Ca2+ATPase of sarcoplasmic reticulum. Expression in developing skeletal muscle. 302 25

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

Three membrane-bound adenosine triphosphatases were investigated for homology in the sequence of four amino acids about the active site of phosphorylation. The ATPases were as follows: sodium-potassium-dependent ATPase from dog kidney, Na,K-ATPase; hydrogen-potassium-dependent ATPase from hog gastric mucosa, H,K-ATPase, an ATPase similar to Na,K-ATPase; and an ATPase activity in the plasma membrane of corn, Zea mays, roots (CR-ATPase), a higher plant ATPase. A membrane preparation containing an ATPase of Acholeplasma laidlawii, a prokaryote, (AL) was also investigated. For most of the experiments, the preparations were phosphorylated from [gamma-32P]ATP, denatured in acid, and subjected to proteolytic digestion. Radioactive phosphopeptides were separated by high voltage paper electrophoresis and characterized by sensitivity to chemical reagents. In gastric H,K-ATPase, the aspartate residue at the active site was determined directly by labeling with [3H]borohydride. A common sequence around the active site was found for Na,K-ATPase, H,K-ATPase, and CR-ATPase. This sequence, -Cys-(Ser/Thr)-Asp(P)-Lys-, is similar to that in the calcium ion-transport ATPase of sarcoplasmic reticulum. The AL membrane preparation showed an acylphosphate that turned over rapidly after a chase of labeled membranes with unlabeled ATP. The corresponding sequence was different from that of the three ATPases. An acylphosphate was on two polypeptides with molecular weights of about 80,000 and 60,000; these appear not to correspond to subunits of a Na+-stimulated ATPase in this organism (Lewis, R. N. A. H., and McElhaney, R. N. (1983) Biochim. Biophys. Acta 735, 113-122).
...
PMID:Structural relatedness of three ion-transport adenosine triphosphatases around their active sites of phosphorylation. 315 36

1. The respiration and aerobic glycolysis of pig ciliary processes in oxygenated phosphate and bicarbonate buffers have been investigated. 2. Significant amounts of lactic acid are produced only in the presence of added glucose, but this does not change the endogenous respiration rate. 3. Succinate and citrate increase the oxygen uptake considerably, but pyruvate has almost no effect; oxaloacetate and fumarate stimulate slightly in the presence of glucose. Aspartate and fumarate together stimulate pyruvate utilization and are oxidized as fast as citrate. 4. Ouabain inhibits the oxidation of glucose and other substrates by limiting the ADP supply from the sodium transport system. Cyanide and azide inhibit respiration and stimulate glycolysis. 5. The transport mechanism depends largely on ATP from oxidative phosphorylation and regulates the rate of respiration and glycolysis by controlling ADP production from the Na(+)-K(+)-activated adenosine triphosphatase.
...
PMID:The tricarboxylic acid cycle and glycolysis in relation to ion transport by the ciliary body. 591 34

Membrane bound (Na,K)-ATPase partially purified from the nauplius larva of the brine shrimp, Artemia salina, was solubilized with the non-ionic detergent C12E8 in the presence of KCl. The addition of KCl was essential for protecting the enzyme against inactivation. With solubilization the enzyme could then be purified to apparent homogeneity. Electron microscopic observation of the purified enzyme revealed a homogeneous population of particles with a diameter of approximately 4 nm. The larger (alpha) subunit of the enzyme formed double bands on sodium dodecyl sulfate-polyacrylamide gels. NH2-terminal sequence analysis of the alpha subunit revealed the possible presence of two isoforms of (Na,K)-ATPase. At the third position a small but distinct amount of lysine was found in addition to glycine, suggesting that the two forms are different from each other at least at the third residue. The NH2-terminal sequence determined is as follows. NH2-Ala-Lys-Gly (Lys)-Lys-Gln-Lys-Lys-Gly-Lys-Asp-Leu-Asn-Glu-Leu-Lys-Lys-Glu-Leu-Asp-Il e-Asp -Phe-His-Lys-Ile-Pro- The sequence is abundant in hydrophilic amino acids, especially lysine, and is quite different from those of vertebrate enzymes reported so far.
...
PMID:Solubilization and purification of Artemia salina (Na,K)-activated ATPase and NH2-terminal amino acid sequence of its larger subunit. 609 82

When the bovine mitochondrial F1-ATPase is inactivated with dicyclohexyl[14C]carbodiimide and then gel-filtered, from 2 to 3 g atoms of 14C are incorporated/mol of enzyme. Prior inactivation of the enzyme by the modification of an essential tyrosine residue with 4-chloro-7-nitrobenzofurazan, a reaction that can be reversed by thiols, does not affect the irreversible inactivation of the ATPase by dicyclohexyl[14C]carbodiimide. During the large scale modification of the F1-ATPase by dicyclohexyl[14C]carbodiimide which led to 70% inactivation, 1.9 g atoms of 14C were incorporated/mol of enzyme. Isolation of the alpha, beta, and gamma subunits from this large scale inactivation revealed that the gram atoms of 14C bound per mol of each of the subunits was: alpha, 0.04; beta, 0.56; and gamma, 0.04. The majority of the radioactivity in a cyanogen bromide digest of the 14C-labeled beta subunit was isolated in a fragment that has the following amino acid sequence: Glu-Leu-Ile-Asn-Asn-Val-Ala-Lys-Ala-His-Gly-Gly-Tyr-Ser-Val-Phe-Ala-Gly-Val-Gly -Glu-Arg-Thr-Arg-Glu-Gly-Asn-Asp-Leu-Tyr-Glu*-His-Met; where Glu* represents the N gamma-glutamyl derivative of dicyclohexyl[14C]urea.
...
PMID:Inactivation of the bovine mitochondrial F1-ATPase with dicyclohexyl[14C]carbodiimide leads to the modification of a specific glutamic acid residue in the beta subunit. 611 57

Bovine heart MF1-ATPase was labeled with limiting amounts of [14C]NBD-C1[( 14C]4-chloro-7-nitro-2,1,3-benzoxadiazole) and the resulting radioactive label on the essential Tyr was stabilized by reduction with zinc in the presence of multidentate ligand EDTA and redox mediator 4,4'-dipyridyl. Subsequent treatment of the labeled protein with cyanogen bromide and separation of the reaction mixture by ion-exchange chromatography yielded essentially only one radioactive polypeptide. Further cleavage of this polypeptide with TPCK-trypsin, lactonization of the terminal homoserine residue and reaction with derivatized polystyrene resin gave a shorter peptide attached to the solid support which contained all the radioactivity. Edman degradation showed that the amino acid sequence of this peptide was Glu . Gly . Asn . Asp . Leu . Tyr . His . Glu . Met, which corresponds to residues 192-200 in the beta subunit of bovine heart MF1-ATPase as determined by Runswick and Walker (1983). Since this specifically labeled Tyr-197 is separated by only one amino acid residue from the essential Glu-199 which was labeled specifically with dicyclohexylcarbodiimide by Yoshida et al. (1982) it seems most likely that both Tyr-197 and Glu-199 play direct roles in the catalytic hydrolysis and synthesis of ATP.
...
PMID:Identification of the initially NBD-labeled essential tyrosine residue in bovine heart MF1-ATPase. 622 29

Glycine at position 9 is replaced by aspartic acid in the mutant b-subunit of Escherichia coli F1F0-ATPase coded for by the uncF476 allele. The mutant b-subunit is not assembled into the membrane in haploid strains carrying the uncF476 allele, but, if the mutant allele is incorporated into a multicopy plasmid, then some assembly of the mutant b-subunit occurs. Two revertant strains were characterized, one of which (AN2030) was a full revertant, the other (AN1953) a partial revertant. DNA sequencing indicated that in strain AN2030 the uncF476 mutation had reverted to give the sequence found in the normal uncF gene. The partial-revertant strain AN1953, however, retained the DNA sequence of the uncF476 allele, and complementation analysis indicated that the second mutation may be in the uncA gene. Membranes prepared from the partial-revertant strain carried out oxidative phosphorylation, although the membranes appeared to be impermeable to protons, and the ATPase activity was sensitive to the inhibitor dicyclohexylcarbodi-imide.
...
PMID:An additional acidic residue in the membrane portion of the b-subunit of the energy-transducing adenosine triphosphatase of Escherichia coli affects both assembly and function. 623 7

The structures and functions of the two alpha-actinin isoforms [R. Kobayashi et al. (1983) Eur. J. Biochem. 133, 607-611] isolated from rabbit longissimus dorsi and psoas muscles were compared. One-dimensional and two-dimensional electrophoretic analyses showed that the two alpha-actinins were different from each other in their subunit chain weights and isoelectric points. The Stokes' radius of the longissimus dorsi and psoas alpha-actinins was 7.4 nm and 7.0 nm, respectively. The amino acid analyses showed that, although the two alpha-actinins are similar in their amino acid compositions, longissimus dorsi alpha-actinin contains more aspartic acid and isoleucine than psoas alpha-actinin but fewer glycine and valine residues. Analysis of the soluble tryptic peptides by two-dimensional mapping revealed that the two alpha-actinins had major differences. These data suggested that the two isoforms are the products of at least two different genes. Despite these differences, both alpha-actinins share a number of common properties. Both alpha-actinins contain a 55-kDa peptide resistant to trypsin. The two proteins show no differences in actomyosin turbidity assays. ATPase assays and F-actin binding assays of alpha-actinin activity. Immunological examination indicates that the two alpha-actinins share antigenic determinants in common.
...
PMID:Different muscle-specific forms of rabbit skeletal muscle alpha-actinin. 623 79

1-Ethyl-3-[3-(dimethylamino)propyl]carbodiimide (EDC), a water-soluble carbodiimide, inhibited ECF1-F0 ATPase activity and proton translocation through F0 when reacted with Escherichia coli membrane vesicles. The site of modification was found to be in subunit c of the F0 portion of the enzyme but did not involve Asp-61, the site labeled by the hydrophobic carbodiimide dicyclohexylcarbodiimide (DCCD). EDC was not covalently incorporated into subunit c in contrast to DCCD. Instead, EDC promoted a cross-link between the C-terminal carboxyl group (Ala-79) and a near-neighbor phosphatidylethanolamine as evidenced by fragmentation of subunit c with cyanogen bromide followed by high-pressure liquid chromatography and thin-layer chromatography.
...
PMID:Modification of the F0 portion of the H+-translocating adenosinetriphosphatase complex of Escherichia coli by the water-soluble carbodiimide 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide and effect on the proton channeling function. 623 82


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---