Journal ArticleDOI
Hydrolysis by horse muscle acylphosphatase of (Ca2+ + Mg2+)-ATPase phosphorylated intermediate.
TLDR
Findings suggest a possible regulatory role of this enzyme in vivo on the calcium transport process by sarcoplasmic reticulum by way of acylphosphatase in rabbit muscle.About:
This article is published in Archives of Biochemistry and Biophysics.The article was published on 1981-04-15. It has received 29 citations till now. The article focuses on the topics: Acylphosphatase & Ca(2+) Mg(2+)-ATPase.read more
Citations
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Journal ArticleDOI
Conformational constraints for amyloid fibrillation: the importance of being unfolded.
TL;DR: In this review, recent findings are surveyed to illustrate that protein fibrillogenesis requires a partially folded conformation, which is relatively unfolded, and shares many structural properties with the pre-molten globule state.
Journal ArticleDOI
Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration, and pH.
Fabrizio Chiti,N. A. J. Van Nuland,Niccolò Taddei,Francesca Magherini,Massimo Stefani,Giampietro Ramponi,Christopher M. Dobson +6 more
TL;DR: The results indicate that acylphosphatase is a relatively unstable protein with a delta G(H2O) of 22 +/- 1 kJ mol-1 at pH 7 and 25 degrees C, suggesting that the overall dimensions of the unfolded state are significantly affected by the number of charges within the polypeptide chain.
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A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure.
Gianfranco Liguri,Guido Camici,Giampaolo Manao,Gianni Cappugi,Paolo Nassi,Alessandra Modesti,Giampietro Ramponi +6 more
TL;DR: A new acylphosphatase from human erythrocytes was isolated by an original purification procedure, and it was found to differ in 44% of the total positions as compared to the human muscle enzyme.
Journal ArticleDOI
Effects of acylphosphatase on the activity of erythrocyte membrane Ca2+ pump.
TL;DR: Findings suggest that, because of its hydrolytic activity on the phosphoenzyme intermediate, acylphosphatase reduces the efficiency of the erythrocyte membrane Ca2+ pump.
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Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Thr42, and Thr46.
Niccolò Taddei,Massimo Stefani,Francesca Magherini,Fabrizio Chiti,Alessandra Modesti,Giovanni Raugei,Giampietro Ramponi +6 more
TL;DR: The reported results strongly support a direct participation of Asn41 to the enzyme catalytic mechanism, indicating that Asn 41 mutants may well represent a useful tool for the investigation of the enzyme physiological function by the negative dominant approach.
References
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Journal ArticleDOI
A Borohydride Reduction Method for Characterization of the Acyl Phosphate Linkage in Proteins and Its Application to Sarcoplasmic Reticulum Adenosine Triphosphatase
Chemda Degani,Paul D. Boyer +1 more
TL;DR: The results demonstrate that the phosphoryl group of sarcoplasmic reticulum ATPase is attached to the β-carboxyl group of an aspartyl residue at the active site.
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Similarity of the Active Site of Phosphorylation of the Adenosine Triphosphatase for Transport of Sodium and Potassium Ions in Kidney to That for Transport of Calcium Ions in the Sarcoplasmic Reticulum of Muscle
TL;DR: Results suggests an active site tripeptide for each enzyme, seryl or threonyl, phosphoaspartyl lysine for each phosphoenzymes.
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Sarcoplasmic reticulum. VII. Properties of a phosphoprotein intermediate implicated in calcium transport.
TL;DR: Hydrolysis of 32P-labeled adenosine triphosphate by skeletal muscle microsomes occurs through a protein-bound phosphate intermediate, which is probably an acyl phosphate.
Journal ArticleDOI
Studies on the Location and Orientation of Proteins in the Sarcoplasmic Reticulum
TL;DR: The adenosine triphosphatase of sarcoplasmic reticulum has been split into three parts by digestion with trypsin and it is suggested that the 60000-mol.
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Structural and chemical asymmetry of the calcium-transporting membranes of the sarcotubular system as revealed by electron microscopy.
Wilhelm Hasselbach,L.-G. Elfvin +1 more
TL;DR: In experiments where the vesicles were incubated with the SH-reagent Hg-phenyl azoferritin, a close packing of ferritin particles at the outer surface of thevesicular membrane was observed, interpreted as indicating a preferred localization of the active sites involved in the calcium transport at theoutersurface of the membrane.