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Journal articles on the topic 'Acylphosphatases'

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Author: Grafiati

Published: 10 March 2023

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1

Modesti, A., N. Taddei, F. Chiti, M. Bucciantini, F. Magherini, S. Rigacci, M. Stefani, G. Raugei, and G. Ramponi. "Properties of Cys21-mutated muscle acylphosphatases." Journal of Protein Chemistry 15, no. 1 (January 1996): 27–34. http://dx.doi.org/10.1007/bf01886808.

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2

Chiarugi, Paola, Giovanni Raugei, Tania Fiaschi, Letizia Taddei, Guido Camici, and Giampietro Ramponi. "Characterization of a novel nucleolytic activity of acylphosphatases." IUBMB Life 40, no. 1 (September 1996): 73–81. http://dx.doi.org/10.1080/15216549600201552.

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3

Taddei, Niccolò, Alessandra Modesti, Monica Bucciantini, Massimo Stefani, Francesca Magherini, Manuela Vecchi, Giovanni Raugei, and Giampietro Ramponi. "Properties of N-terminus truncated and C-terminus mutated muscle acylphosphatases." FEBS Letters 362, no. 2 (April 3, 1995): 175–79. http://dx.doi.org/10.1016/0014-5793(95)00236-3.

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4

Berti, Andrea, Maurizio Stefani, Donatella Degl'Innocenti, Marco Ruggiero, Vincenzo Chiarugi, and Giampiero Ramponi. "Effect of exogenously added acylphosphatases on inositol lipid metabolism in human platelets." FEBS Letters 235, no. 1-2 (August 1, 1988): 229–32. http://dx.doi.org/10.1016/0014-5793(88)81268-7.

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5

PAOLI, Paolo, Guido CAMICI, Giampaolo MANAO, Elisa GIANNONI, and Giampietro RAMPONI. "Acylphosphatase possesses nucleoside triphosphatase and nucleoside diphosphatase activities." Biochemical Journal 349, no. 1 (June 26, 2000): 43–49. http://dx.doi.org/10.1042/bj3490043.

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We have demonstrated that acylphosphatase possesses ATP-diphosphohydrolase (apyrase-like) activity. In fact, acylphosphatase first catalyses the hydrolysis of the γ-phosphate group of nucleoside triphosphates, and then attacks the β-phosphate group of the initially produced nucleoside diphosphates, generating nucleoside monophosphates. In constrast, it binds nucleoside monophosphates but does not catalyse their hydrolyses. The calculated kcat values for the nucleoside triphosphatase activity of acylphosphatase are of the same order of magnitude as those displayed by certain G-proteins. An acidic environment enhances the apyrase-like activity of acylphosphatase. The true nucleotide substrates of acylphosphatase are free nucleoside di- and triphosphates, as indicated by the Mg2+ ion inhibition of the activity. We have also demonstrated that, although nucleoside triphosphates are still hydrolysed at pH 7.2 and 37 °C, in the presence of millimolar Mg2+ concentrations this occurs at a lower rate. Taken together with the previously observed strong increase of acylphosphatase levels during induced cell differentiation, our findings suggest that acylphosphatase plays an active role in the differentiation process (as well as in other processes, such as apoptosis) by modulating the ratio between the cellular levels of nucleoside diphosphates and nucleoside triphosphates.

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6

Chiarugi, P., G. Raugei, R. Marzocchini, T. Fiaschi, C. Ciccarelli, A. Berti, and G. Ramponi. "Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone." Biochemical Journal 311, no. 2 (October 15, 1995): 567–73. http://dx.doi.org/10.1042/bj3110567.

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The modulation of expression of the skeletal muscle and erythrocyte acylphosphatase isoenzymes by thyroid hormone has been investigated. Our results indicate a differential regulation of the two enzymic isoforms by tri-iodothyronine (T3) in K562 cells in culture: an increase in the specific mRNA during T3-stimulation is shown only for the skeletal muscle isoenzyme. A fast and transient T3 induction of the accumulation of the specific mRNA can be observed, reaching a maximum 8 h after hormone treatment and then rapidly decreasing almost to the steady-state level after 24 h. A nuclear run-on assay was performed to explore the mechanisms of this regulation. These studies indicate that T3 induction of skeletal muscle acylphosphatase mRNA is due, at least in part, to a fast and transient increase in the rate of gene transcription, within 4 h after hormone administration. A very rapid decrease is then observed within a further 2 h. T3-dependent accumulation of the mRNA for the skeletal muscle acylphosphatase requires ongoing protein synthesis, as confirmed by inhibition with cycloheximide or puromycin. These findings indicate that the transcriptional regulation of the gene may be indirect.

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7

SAUDEK, V., M. R. WORMALD, R. J. P. WILLIAMS, and G. RAMPONI. "N.m.r. study of acylphosphatase." Biochemical Society Transactions 15, no. 5 (October 1, 1987): 872–74. http://dx.doi.org/10.1042/bst0150872.

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8

Pastore, Annalisa, Vladimir Saudek, Giampietro Ramponi, and Robert J. P. Williams. "Three-dimensional structure of acylphosphatase." Journal of Molecular Biology 224, no. 2 (March 1992): 427–40. http://dx.doi.org/10.1016/0022-2836(92)91005-a.

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9

Nediani, Chiara, Alessandra Celli, Claudia Fiorillo, Vanessa Ponziani, Lara Giannini, and Paolo Nassi. "Acylphosphatase interferes with SERCA2a–PLN association." Biochemical and Biophysical Research Communications 301, no. 4 (February 2003): 948–51. http://dx.doi.org/10.1016/s0006-291x(03)00078-0.

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10

Stefani, M., A. Berti, G. Camici, G. Manao, D. Degl'Innocenti, G. Prakash, R. Marzocchini, and G. Ramponi. "Horse brain acylphosphatase: Purification and characterization." FEBS Letters 236, no. 1 (August 15, 1988): 209–16. http://dx.doi.org/10.1016/0014-5793(88)80316-8.

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11

Plakoutsi, Georgia, Niccolò Taddei, Massimo Stefani, and Fabrizio Chiti. "Aggregation of the Acylphosphatase fromSulfolobus solfataricus." Journal of Biological Chemistry 279, no. 14 (January 14, 2004): 14111–19. http://dx.doi.org/10.1074/jbc.m312961200.

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12

Stefani, Massimo, Alessandra Modesti, Guido Camici, Giampaolo Manao, Gianni Cappugi, Andrea Berti, and Giampietro Ramponi. "Duck skeletal muscle acylphosphatase: Primary structure." Journal of Protein Chemistry 5, no. 5 (October 1986): 307–21. http://dx.doi.org/10.1007/bf01025960.

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13

Mizuno, Yusuke, Yoichi Ohba, Hisakazu Fujita, Yoshikazu Kanesaka, Takiko Tamura, and Hiroyuki Shiokawa. "Distribution and classification of acylphosphatase isozymes." Archives of Biochemistry and Biophysics 278, no. 2 (May 1990): 437–43. http://dx.doi.org/10.1016/0003-9861(90)90282-4.

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14

FUJTTA, Hisakazu, Yusuke MIZUNO, and Hiroyuki SHIOKAWA. "Purification and Properties of Porcine Testis Acylphosphatase." Journal of Biochemistry 102, no. 6 (December 1987): 1405–14. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122186.

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15

Degl'Innocenti, Donatella, Matteo Ramazzotti, Riccardo Marzocchini, Fabrizio Chiti, Giovanni Raugei, and Giampietro Ramponi. "Characterization of a novel Drosophila melanogaster acylphosphatase." FEBS Letters 535, no. 1-3 (January 10, 2003): 171–74. http://dx.doi.org/10.1016/s0014-5793(02)03901-7.

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16

Stefani, M., N. Taddei, and G. Ramponi. "Insights into acylphosphatase structure and catalytic mechanism." Cellular and Molecular Life Sciences 53, no. 2 (February 1997): 141–51. http://dx.doi.org/10.1007/pl00000585.

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17

Taddei, Niccolo', Matthias Buck, R. William Broadhurst, Massimo Stefani, Giampietro Ramponi, and Christopher M. Dobson. "Equilibrium Unfolding Studies of Horse Muscle Acylphosphatase." European Journal of Biochemistry 225, no. 3 (November 1994): 811–17. http://dx.doi.org/10.1111/j.1432-1033.1994.0811b.x.

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18

Manao, Giampaolo, Gianni Cappugi, Alessandra Modesti, Massimo Stefani, Riccardo Marzocchini, Donatella Degl'Innocenti, and Guido Camici. "Guinea pig acylphosphatase: The amino acid sequence." Journal of Protein Chemistry 7, no. 4 (August 1988): 417–26. http://dx.doi.org/10.1007/bf01024889.

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19

Mizuno, Yusuke, Yoichi Ohba, Hisakazu Fujita, Yoshikazu Kanesaka, Takiko Tamura, and Hiroyuki Shiokawa. "Activity staining of acylphosphatase after gel electrophoresis." Analytical Biochemistry 183, no. 1 (November 1989): 46–49. http://dx.doi.org/10.1016/0003-2697(89)90169-3.

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20

PAOLI, Paolo, Guido CAMICI, Giampaolo MANAO, Elisa GIANNONI, and Giampietro RAMPONI. "Acylphosphatase possesses nucleoside triphosphatase and nucleoside diphosphatase activities." Biochemical Journal 349, no. 1 (July 1, 2000): 43. http://dx.doi.org/10.1042/0264-6021:3490043.

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21

PAOLI, Paolo, Tania FIASCHI, Paolo CIRRI, Guido CAMICI, Giampaolo MANAO, Gianni CAPPUGI, Giovanni RAUGEI, Gloriano MONETI, and Giampietro RAMPONI. "Mechanism of acylphosphatase inactivation by Woodward's reagent K." Biochemical Journal 328, no. 3 (December 15, 1997): 855–61. http://dx.doi.org/10.1042/bj3280855.

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The organ common-type (CT) isoenzyme of acylphosphatase is inactivated by Woodward's reagent K (WRK) (N-ethyl-5-phenylisoxazolium-3ʹ-sulphonate) at pH 6.0. The inactivation reaction follows apparent pseudo first-order kinetics. The dependence of the reciprocal of the pseudo first-order kinetic constant (kobs) on the reciprocal WRK concentration reveals saturation kinetics, suggesting that the WRK forms a reversible complex with the enzyme before causing inactivation. Competitive inhibitors, such as inorganic phosphate and ATP, protect the enzyme from WRK inactivation, suggesting that this reagent acts at or near to the enzyme active site. The reagent-enzyme adduct, which elicits a strong absorption band with λmax at 346 nm, was separated from unreacted enzyme by reverse phase HPLC and the modified protein was cleaved with endoproteinase Glu-C to produce fragments. The HPLC fractionation gave two reagent-labelled peptides (peak 1 and peak 2) that were analysed by ion-spray MS and sequenced. The former is VFFRKHTQAE (residues 20-29 of human CT acylphosphatase) and the latter IFGKVQGVFFRKHTQAE (residues 13-29). MS demonstrated that both peptides are WRK adducts. A fragment ion with m/z of 1171, which is present in the mass spectrum of peak 1, has been identified as a WRK adduct of the peptide fragment 20-26. The λmax at 346 nm of WRK adduct suggests that the modified residue is His-25. Five recombinant enzymes mutated in residues included in the 20-29 polypeptide stretch have been produced. Analysis of their reactivities with WRK demonstrates that His-25 is the molecular target of the reagent as its modification causes the inactivation of the enzyme. Since both His-25 → Gln and His-25 → Phe mutants maintain high catalytic activity, we suggest that the observed enzyme inactivation is caused by the reagent (covalently bound to His-25), which shields the active site.

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22

Chiarugi, Paola, Donatella Degl'Innocenti, Letizia Taddei, Giovanni Raugei, Andrea Berti, Stefania Rigacci, and Giampietro Ramponi. "Acylphosphatase is involved in differentiation of K562 cells." Cell Death & Differentiation 4, no. 4 (May 1997): 334–40. http://dx.doi.org/10.1038/sj.cdd.4400230.

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23

KIZAKI, Takako, Yusuke MIZUNO, Toshihide TAKASAWA, and Hiroyuki SHIOKAWA. "Antigenic Determinants of Acylphosphatase from Porcine Skeletal Muscle." Journal of Biochemistry 97, no. 4 (April 1985): 1143–54. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a135159.

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24

Liguri, Gianfranco, Paolo Nassi, Donatella Degl'innocenti, Elda Tremori, Chiara Nediani, Andrea Berti, and Giampietro Ramponi. "Acylphosphatase levels of human erythrocytes during cell ageing." Mechanisms of Ageing and Development 39, no. 1 (June 1987): 59–67. http://dx.doi.org/10.1016/0047-6374(87)90086-8.

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25

Nassi, Paolo, Gianfranco Liguri, Chiara Nediani, Niccoló Taddei, Patrizia Piccinni, Donatella Degl'Innocenti, Riccardo G. Gheri, and Giampietro Ramponi. "Increased acylphosphatase levels in erythrocytes from hyperthyroid patients." Clinica Chimica Acta 183, no. 3 (August 1989): 351–58. http://dx.doi.org/10.1016/0009-8981(89)90370-7.

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26

Saudek, V., R. J. P. Williams, and G. Ramponi. "Secondary structure of acylphosphatase from rabbit skeletal muscle." Journal of Molecular Biology 199, no. 1 (January 1988): 233–37. http://dx.doi.org/10.1016/0022-2836(88)90394-4.

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27

Pazzagli, Luigia, Gianni Cappugi, Guido Camici, Giampaolo Manao, and Giampietro Ramponi. "Bovine testis acylphosphatase: Purification and amino acid sequence." Journal of Protein Chemistry 12, no. 5 (October 1993): 593–601. http://dx.doi.org/10.1007/bf01025124.

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28

MINOWA, Osamu, Yoichi OHBA, Yusuke MIZUNO, and Hiroyuki SHIOKAWA. "The Primary Structure of Chicken Muscle Acylphosphatase Isozyme Ch1." Journal of Biochemistry 102, no. 5 (November 1987): 1213–20. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122160.

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29

OHBA, Yoichi, Osamu MINOWA, Yusuke MIZUNO, and Hiroyuki SHIOKAWA. "The Primary Structure of Chicken Muscle Acylphosphatase Isozyme CH2." Journal of Biochemistry 102, no. 5 (November 1987): 1221–29. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122161.

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30

Raugei, G., P. Chiarugi, D. Degl'Innocenti, A. Berti, L. Taddei, S. Rigacci, and G. Ramponi. "ACYLPHOSPHATASE LEVEL IN K562 CELLS IS CORRELATED WITH DIFFERENTIATION." Biochemical Society Transactions 24, no. 4 (November 1, 1996): 552S. http://dx.doi.org/10.1042/bst024552sa.

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31

Nediani, Chiara, Claudia Fiorillo, Elena Marchetti, Alessandra Pacini, Gianfranco Liguri, and Paolo Nassi. "Stimulation of Cardiac Sarcoplasmic Reticulum Calcium Pump by Acylphosphatase." Journal of Biological Chemistry 271, no. 32 (August 9, 1996): 19066–73. http://dx.doi.org/10.1074/jbc.271.32.19066.

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32

MIZUNO, Yusuke, Morihiro YAMAZAKI, Toshihide TAKASAWA, Takako KIZAKI, and Hiroyuki SHIOKAWA. "Amino Acid Sequence of Acylphosphatase from Porcine Skeletal Muscle." Journal of Biochemistry 97, no. 4 (April 1985): 1135–42. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a135158.

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33

KIZAKI, Takako, Toshihide TAKASAWA, Yusuke MIZUNO, and Hiroyuki SHIOKAWA. "Amino Acid Sequence of Acylphosphatase from Rabbit Skeletal Muscle." Journal of Biochemistry 97, no. 4 (April 1985): 1155–61. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a135160.

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34

OHBA, Yoichi, Yusuke MIZUNO, Toshihide TAKASAWA, and Hiroyuki SHIOKAWA. "Two Isozymes of Chicken Muscle Acylphosphatase: Purification and Properties." Journal of Biochemistry 98, no. 4 (October 1985): 909–19. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a135370.

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35

Thunnissen, Marjolein MGM, Niccolo’ Taddei, Gianfranco Liguri, Giampietro Ramponi, and Pär Nordlund. "Crystal structure of common type acylphosphatase from bovine testis." Structure 5, no. 1 (January 1997): 69–79. http://dx.doi.org/10.1016/s0969-2126(97)00167-6.

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36

Tamura, Takiko, Yusuke Mizuno, and Hiroyuki Shiokawa. "Chemical modification of arginine residues of porcine muscle acylphosphatase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 870, no. 2 (March 1986): 234–41. http://dx.doi.org/10.1016/0167-4838(86)90227-x.

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37

Hu, Jicheng, Dan Li, Xiao-Dong Su, Changwen Jin, and Bin Xia. "Solution structure and conformational heterogeneity of acylphosphatase fromBacillus subtilis." FEBS Letters 584, no. 13 (May 4, 2010): 2852–56. http://dx.doi.org/10.1016/j.febslet.2010.04.069.

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38

Nassi, P., C. Nediani, G. Liguri, N. Taddei, M. Ruggiero, and G. Ramponi. "Effect of acylphosphatase on human erythrocyte membrane Ca2+-ATPase." Biochemical and Biophysical Research Communications 168, no. 2 (April 1990): 651–58. http://dx.doi.org/10.1016/0006-291x(90)92370-f.

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39

Pagano, Katiuscia, Matteo Ramazzotti, Paolo Viglino, Gennaro Esposito, Donatella Degl’Innocenti, Niccolò Taddei, and Alessandra Corazza. "NMR solution structure of the acylphosphatase from Escherichia coli." Journal of Biomolecular NMR 36, no. 3 (October 5, 2006): 199–204. http://dx.doi.org/10.1007/s10858-006-9073-2.

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40

Berti, Andrea, Elda Tremori, Luigia Pazzagli, Donatella Degl'Innocenti, Guido Camici, Gianni Cappugi, Giampaolo Manao, and Giampietro Ramponi. "Rat muscle acylphosphatase: Purification, amino sequence, and immunological characterization." Journal of Protein Chemistry 10, no. 1 (February 1991): 91–102. http://dx.doi.org/10.1007/bf01024659.

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41

Stefani, M., D. Degl'Innocenti, A. Berti, R. Marzocchini, G. Camici, G. Manao, and G. Ramponi. "Identification of three continuous antigenic sites in horse muscle acylphosphatase." Journal of Protein Chemistry 6, no. 6 (December 1987): 479–87. http://dx.doi.org/10.1007/bf00276734.

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42

马, 雪宁. "Single Molecule Magnetic Tweezers Study of Unfolding Kinetics of Acylphosphatase." Biophysics 10, no. 02 (2022): 22–30. http://dx.doi.org/10.12677/biphy.2022.102003.

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43

MIYAZONO, Ken-ichi, Yoriko SAWANO, and Masaru TANOKURA. "Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3." Proceedings of the Japan Academy, Series B 80, no. 9 (2004): 439–42. http://dx.doi.org/10.2183/pjab.80.439.

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44

Yeung, Rachel C. Y., Sonia Y. Lam, and Kam-Bo Wong. "Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase." Acta Crystallographica Section F Structural Biology and Crystallization Communications 62, no. 1 (December 23, 2005): 80–82. http://dx.doi.org/10.1107/s174430910504145x.

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45

PAOLI, Paolo, Paolo CIRRI, Lucia CAMICI, Giampaolo MANAO, Gianni CAPPUGI, Gloriano MONETI, Giuseppe PIERACCINI, Guido CAMICI, and Giampietro RAMPONI. "Common-type acylphosphatase: steady-state kinetics and leaving-group dependence." Biochemical Journal 327, no. 1 (October 1, 1997): 177–84. http://dx.doi.org/10.1042/bj3270177.

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A number of acyl phosphates differing in the structure of the acyl moiety (as well as in the leaving-group pKa of the acids produced in hydrolysis) have been synthesized. The Km and Vmax values for the bovine common-type acylphosphatase isoenzyme have been measured at 25 °C and pH 5.3. The values of kcat differ widely in relation to the different structures of the tested acyl phosphates: linear relationships between log kcat and the leaving group pKa, as well as between log kcat/Km and the leaving-group pKa, were observed. On the other hand, the Km values of the different substrates are very close to each other, suggesting that the phosphate moiety of the substrate is the main chemical group interacting with the enzyme active site in the formation of the enzyme–substrate Michaelis complex. The enzyme does not catalyse transphosphorylation between substrate and concentrated nucleophilic acceptors (glycerol and methanol); nor does it catalyse H218O–inorganic phosphate oxygen exchange. It seems that no phosphoenzyme intermediate is formed in the catalytic pathway. Furthermore, during the enzymic hydrolysis of benzoyl phosphate in the presence of 18O-labelled water, only inorganic phosphate (and not benzoate) incorporates 18O, suggesting that no acyl enzyme is formed transiently. All these findings, as well as the strong dependence of kcat upon the leaving group pKa, suggest that neither a nucleophilic enzyme group nor general acid catalysis are involved in the catalytic pathway. The enzyme is competitively inhibited by Pi, but it is not inhibited by the carboxylate ions produced during substrate hydrolysis, suggesting that the last step of the catalytic process is the release of Pi. The activation energy values for the catalysed and spontaneous hydrolysis of benzoyl phosphate have been determined.

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46

Nediani, Chiara, Claudia Fiorillo, Elena Marchetti, Renzo Bandinelli, Donatella Degl'Innocenti, and Paolo Nassi. "Acylphosphatase: A Potential Modulator of Heart Sarcolemma Na+,K+ Pump." Biochemistry 34, no. 20 (May 23, 1995): 6668–74. http://dx.doi.org/10.1021/bi00020a012.

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47

Giannoni, E., P. Cirri, P. Paoli, T. Fiaschi, G. Camici, G. Manao, G. Raugei, and G. Ramponi. "Acylphosphatase Is a Strong Apoptosis Inducer in HeLa Cell Line." Molecular Cell Biology Research Communications 3, no. 5 (May 2000): 264–70. http://dx.doi.org/10.1006/mcbr.2000.0228.

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48

Fusco, Giuliana, Alfonso De Simone, Shang-Te Danny Hsu, Francesco Bemporad, Michele Vendruscolo, Fabrizio Chiti, and Christopher M. Dobson. "1H, 13C and 15N resonance assignments of human muscle acylphosphatase." Biomolecular NMR Assignments 6, no. 1 (June 5, 2011): 27–29. http://dx.doi.org/10.1007/s12104-011-9318-1.

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49

Stefani, M., D. Degl'Innocenti, A. Berti, G. Cappugi, G. Manao, G. Camici, and G. Ramponi. "Purification and characterization of acylphosphatase erythrocyte isoenzyme from turkey muscle." Journal of Protein Chemistry 9, no. 5 (October 1990): 633–40. http://dx.doi.org/10.1007/bf01025017.

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50

Dolfi, Fabrizio, Amancio Carnero, Antonio Cuadrado, Giampietro Ramponi, and Juan Carlos Lacal. "Acylphosphatase synergizes with progesterone during maturation of Xenopus laevis oocytes." FEBS Letters 327, no. 3 (August 2, 1993): 265–70. http://dx.doi.org/10.1016/0014-5793(93)81001-g.

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