Littérature scientifique sur le sujet « Acylphosphatase »
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Articles de revues sur le sujet "Acylphosphatase"
PAOLI, Paolo, Guido CAMICI, Giampaolo MANAO, Elisa GIANNONI et Giampietro RAMPONI. « Acylphosphatase possesses nucleoside triphosphatase and nucleoside diphosphatase activities ». Biochemical Journal 349, no 1 (26 juin 2000) : 43–49. http://dx.doi.org/10.1042/bj3490043.
Texte intégralSAUDEK, V., M. R. WORMALD, R. J. P. WILLIAMS et G. RAMPONI. « N.m.r. study of acylphosphatase ». Biochemical Society Transactions 15, no 5 (1 octobre 1987) : 872–74. http://dx.doi.org/10.1042/bst0150872.
Texte intégralChiarugi, P., G. Raugei, R. Marzocchini, T. Fiaschi, C. Ciccarelli, A. Berti et G. Ramponi. « Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone ». Biochemical Journal 311, no 2 (15 octobre 1995) : 567–73. http://dx.doi.org/10.1042/bj3110567.
Texte intégralPastore, Annalisa, Vladimir Saudek, Giampietro Ramponi et Robert J. P. Williams. « Three-dimensional structure of acylphosphatase ». Journal of Molecular Biology 224, no 2 (mars 1992) : 427–40. http://dx.doi.org/10.1016/0022-2836(92)91005-a.
Texte intégralNediani, Chiara, Alessandra Celli, Claudia Fiorillo, Vanessa Ponziani, Lara Giannini et Paolo Nassi. « Acylphosphatase interferes with SERCA2a–PLN association ». Biochemical and Biophysical Research Communications 301, no 4 (février 2003) : 948–51. http://dx.doi.org/10.1016/s0006-291x(03)00078-0.
Texte intégralStefani, M., A. Berti, G. Camici, G. Manao, D. Degl'Innocenti, G. Prakash, R. Marzocchini et G. Ramponi. « Horse brain acylphosphatase : Purification and characterization ». FEBS Letters 236, no 1 (15 août 1988) : 209–16. http://dx.doi.org/10.1016/0014-5793(88)80316-8.
Texte intégralPlakoutsi, Georgia, Niccolò Taddei, Massimo Stefani et Fabrizio Chiti. « Aggregation of the Acylphosphatase fromSulfolobus solfataricus ». Journal of Biological Chemistry 279, no 14 (14 janvier 2004) : 14111–19. http://dx.doi.org/10.1074/jbc.m312961200.
Texte intégralStefani, Massimo, Alessandra Modesti, Guido Camici, Giampaolo Manao, Gianni Cappugi, Andrea Berti et Giampietro Ramponi. « Duck skeletal muscle acylphosphatase : Primary structure ». Journal of Protein Chemistry 5, no 5 (octobre 1986) : 307–21. http://dx.doi.org/10.1007/bf01025960.
Texte intégralMizuno, Yusuke, Yoichi Ohba, Hisakazu Fujita, Yoshikazu Kanesaka, Takiko Tamura et Hiroyuki Shiokawa. « Distribution and classification of acylphosphatase isozymes ». Archives of Biochemistry and Biophysics 278, no 2 (mai 1990) : 437–43. http://dx.doi.org/10.1016/0003-9861(90)90282-4.
Texte intégralFUJTTA, Hisakazu, Yusuke MIZUNO et Hiroyuki SHIOKAWA. « Purification and Properties of Porcine Testis Acylphosphatase ». Journal of Biochemistry 102, no 6 (décembre 1987) : 1405–14. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122186.
Texte intégralThèses sur le sujet "Acylphosphatase"
Chiti, Fabrizio. « Folding studies of acylphosphatase ». Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.326073.
Texte intégralBemporad, Francesco. « Folding and aggregation studies in the acylphosphatase-like family / ». Firenze : Firenze University Press, 2009. http://digital.casalini.it/9788884539465.
Texte intégralGuan, Xiao. « NMR approaches to protein conformation and backbone dynamics studies on hyperthermophilic acylphosphatase and neuropeptide secretoneurin / ». Click to view the E-thesis via HKUTO, 2010. http://sunzi.lib.hku.hk/hkuto/record/B44079230.
Texte intégralRAMAZZOTTI, MATTEO. « Advances in acylphosphatase studies : phylogenesis, novel enzymes and amyloid aggregation ». Doctoral thesis, 2006. http://hdl.handle.net/2158/684337.
Texte intégral« Crystal structure of human common-type acylphosphatase and insights into enzyme-substrate interaction ». 2008. http://library.cuhk.edu.hk/record=b5893591.
Texte intégralThesis (M.Phil.)--Chinese University of Hong Kong, 2008.
Includes bibliographical references (leaves 112-122).
Abstracts in English and Chinese.
Acknowledgments --- p.I
Abstract --- p.II
摘要 --- p.III
Content --- p.IV
Abbreviations and symbols --- p.XI
List of tables and figures --- p.XV
Chapter Chapter 1 --- Introduction --- p.1
Chapter 1.1 --- Acylphosphatase --- p.1
Chapter 1.2 --- Human acylphosphatase --- p.4
Chapter 1.3 --- Hyperthermophilic Pyrococcus horikoshii acylphosphatase --- p.5
Chapter 1.4 --- Human common-type acylphosphatase as a mesophilic homologue of Pyrococcus horikoshii acylphosphatase --- p.8
Chapter 1.5 --- Enzyme-substrate interaction of acylphosphatase --- p.9
Chapter Chapter 2 --- Materials and methods --- p.10
Chapter 2.1 --- Preparation of Escherichia coli competent cells --- p.10
Chapter 2.2 --- SDS-polyacrylamide gel electrophoresis --- p.11
Chapter 2.2.1 --- Preparation of polyacrylamide gel --- p.11
Chapter 2.2.2 --- SDS-polyacrylamide gel electrophoresis (SDS-PAGE) --- p.12
Chapter 2.2.3 --- Staining of protein in polyacrylamide gel by Coommassie Brillant Blue R250 --- p.12
Chapter 2.3 --- Expression and purification of Protein --- p.13
Chapter 2.3.1 --- "General bacterial culture, harvesting and lysis" --- p.13
Chapter 2.3.2 --- Purification of acylphosphatase --- p.14
Chapter 2.3.2.1 --- Ion-exchange chromatography --- p.14
Chapter 2.3.2.2 --- Size excision chromatography --- p.15
Chapter 2.3.3 --- Protein concentration determination --- p.16
Chapter 2.4 --- X-ray crystallography --- p.17
Chapter 2.4.1 --- Crystallization of Hu CT AcP --- p.17
Chapter 2.4.2 --- Model building and structural refinement --- p.18
Chapter 2.4.3 --- Crystallization of Hu CT AcP -substate analogue complex --- p.19
Chapter 2.5 --- Enzymatic Assay --- p.21
Chapter 2.5.1 --- Preparation of benzoyl phosphate --- p.21
Chapter 2.5.2 --- Purity check of the BP synthesized --- p.22
Chapter 2.5.3 --- Determination of kinetic parameters of Hu CT AcP --- p.25
Chapter 2.5.4 --- Determination of Ki value of substrate analogue --- p.27
Chapter 2.6 --- Isothermal titration calorimetry --- p.28
Chapter 2.7 --- Reagents and Buffers --- p.30
Chapter 2.7.1 --- Reagent for competent cell preparation --- p.30
Chapter 2.7.2 --- Media for bacterial culture --- p.31
Chapter 2.7.3 --- Reagent for SDS-PAGE --- p.32
Chapter 2.7.4 --- Buffer for AcP purification --- p.33
Chapter 2.7.5 --- Buffer for enzymatic assay and ITC --- p.33
Chapter Chapter 3 --- Structural determination of human common-type acylphosphatase --- p.34
Chapter 3.1 --- Introduction --- p.34
Chapter 3.2 --- Expression and purification of Hu CT AcP --- p.35
Chapter 3.3 --- Structure of Hu CT AcP was determined by X-ray crystallography --- p.37
Chapter 3.3.1 --- Crystallization of Hu CT AcP --- p.37
Chapter 3.3.2 --- Model building and structural refinement --- p.41
Chapter 3.3.3 --- Hu CT AcP shares a same α/β sandwich fold structure as other AcP --- p.43
Chapter 3.4 --- Discussion --- p.46
Chapter 3.4.1 --- Active site structure of Hu CT AcP is the same as those of bovine CT AcP and Ph AcP --- p.46
Chapter 3.4.2 --- Absence of salt bridge between the active site residue and the C-terminal may contribute to the higher catalytic efficiency of Hu CT AcP --- p.52
Chapter Chapter 4 --- Characterization of interaction between acylphosphatase and substrate analogues --- p.56
Chapter 4.1 --- Introduction --- p.56
Chapter 4.2 --- Selected substrate analogues --- p.57
Chapter 4.3 --- Characterization of AcP-substrate analogue interaction by enzymatic assay --- p.59
Chapter 4.3.1 --- Enzyme kinetics of Hu CT AcP was determined by the continuous optical assay of BP hydrolysis --- p.59
Chapter 4.3.2 --- Substrate analogues were found to be competitive inhibitor to the AcP-catalyzed BP hydrolysis --- p.61
Chapter 4.3.3 --- S-BA was the best competitive inhibitor against AcP-catalyzed BP hydrolysis --- p.64
Chapter 4.3.4 --- S-BA was shown to be a competitive inhibitor for both Hu CT and Ph AcP --- p.66
Chapter 4.4 --- Characterization of AcP-substrate analogue interaction by thermodynamic study --- p.68
Chapter 4.4.1 --- Enthalpy change was observed for the association between substrate analogue and AcP --- p.68
Chapter 4.4.2 --- S-BA was shown to bind Hu CT AcP with high affinity in ITC study --- p.68
Chapter 4.5 --- S-BA was found to be the best substrate analogue for AcP --- p.72
Chapter 4.6 --- Discussion --- p.73
Chapter 4.6.1 --- Structure-affinity study of substrate analogue reveals chemical structures essential to interaction with AcP --- p.73
Chapter 4.6.2 --- Structure-affinity study of substrate analogues is consistent with docking model of AcP with acetyl phosphate --- p.75
Chapter 4.6.3 --- Validation of docking model by crystal complex structure --- p.78
Chapter 4.6.4 --- Structural basis of substrate inhibition in Hu CT AcP --- p.80
Chapter 4.6.4.1 --- Substrate inhibition is observed in Hu CT AcP --- p.80
Chapter 4.6.4.2 --- Non-productive binding and substrate inhibition in AcP --- p.80
Chapter Chapter 5 --- Investigation on the effect of salt bridge on acylphosphatase- substrate analogue interaction --- p.84
Chapter 5.1 --- Introduction --- p.84
Chapter 5.2 --- Thermodynamic study on the binding of S-BA with AcPs --- p.87
Chapter 5.2.1 --- Determination of thermodynamic parameters of interaction between AcP and substrate analogue --- p.87
Chapter 5.2.2 --- Determination of thermodynamic parameters as a function of temperature --- p.90
Chapter 5.3 --- Discussion --- p.93
Chapter 5.3.1 --- The presence of salt bridge leads to a reduced flexibility at the substrate binding active site --- p.93
Chapter 5.3.2 --- The single salt bridge reduces the flexibility of active site in both study on thermodynamics of binding and thermodynamics of activation --- p.94
Chapter 5.3.3 --- Temperature dependence of the thermodynamic parameters and heat capacity change ΔCp --- p.97
Chapter 5.3.3.1 --- Change in heat capacity reveals the nature of the complex interface --- p.97
Chapter 5.3.3.2 --- Determination of heat capacity change ΔCp --- p.98
Chapter Chapter 6 --- Structural determination of acylphosphatase-substrate analogue complex --- p.102
Chapter 6.1 --- Introduction --- p.102
Chapter 6.2 --- Soaking and cocrystallization failed to give cocrystal structure of Hu CT AcP and S-BA --- p.103
Chapter 6.4 --- Discussion --- p.106
Chapter 6.4.1 --- Hu CT AcP and S-BA is not compatible with cocrystal formation --- p.106
Chapter 6.5 --- Future prospect --- p.107
Chapter 6.5.1 --- Structure determination by NMR spectroscopy --- p.107
Chapter 6.5.2 --- Structure determination of AcP with aluminofluoride complexes --- p.108
Chapter Chapter 7 --- Conclusion --- p.109
Reference --- p.112
MOTAMEDI-SHAD, NEDA. « Amyloid formation by the model protein human muscle acylphosphatase in the presence of the glycosamminoglycan heparan sulfate ». Doctoral thesis, 2010. http://hdl.handle.net/2158/599239.
Texte intégral« A high-resolution study of the structure and conformational stability of Pyrococcus horikoshii acylphosphatase in ionic liquid 1-ethyl-3-methylimidazolium tetrafluoroborate by NMR spectroscopy ». 2013. http://library.cuhk.edu.hk/record=b5549251.
Texte intégralThe extensive application of ionic liquid in biocatalysis and protein chemistry in the past decade arouses interest in the characterization of protein behavior in ionic liquid. This study demonstrates the use of multi-dimensional nuclear magnetic resonance (NMR) spectroscopy to investigate the structure and conformational stability of protein in ionic liquid at a high resolution for the first time, with Pyrococcus horikoshii acylphosphatase (PhAcP) and 50% (v/v) 1-ethyl-3-methylimidazolium tetrafluoroborate ([EMIM][BF₄]) as a study model. The backbone amide resonances of PhAcP in 50% (v/v) [EMIM][BF₄] were assigned in order to obtain the chemical shifts of ¹³C[superscript α], ¹³C[superscript β], ¹³CO, ¹⁵N, HN and H[superscript α] of each assigned residue. The estimation of secondary structure by the ¹³C secondary shift analysis and the nuclear Overhauser effect (NOE) connectivities observed within secondary structures together suggest that PhAcP has secondary structures arranged in native-like topology and there is no major alteration in the tertiary structure in 50% (v/v) [EMIM][BF₄]. Guanidine thiocyanate (GdnSCN)-induced denaturation was performed at 318K, 328K and 338K and monitored by 2D ¹H-¹⁵N HSQC experiments to study the conformational stability of PhAcP in 50% (v/v) [EMIM][BF₄]. The overlapping denaturation curves and consistent [GdnSCN]₁[subscript /]₂ values obtained at each temperature indicate no observable trend of stability alteration.
Detailed summary in vernacular field only.
Lee, Tsz Ying.
Thesis (M.Phil.)--Chinese University of Hong Kong, 2013.
Includes bibliographical references (leaves 57-63).
Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web.
Abstracts also in Chinese.
Abstract --- p.i
摘要 --- p.ii
Acknowledgements --- p.iii
Contents --- p.iv
Abbreviations --- p.vii
List of Figures --- p.viii
List of Tables --- p.ix
Chapter Chapter 1 --- Introduction --- p.1
Chapter 1.1 --- Introduction to ionic liquid --- p.1
Chapter 1.1.1 --- Ionic liquid as reaction medium, co-solvent and additive in biocatalysis and protein chemistry --- p.1
Chapter 1.1.2 --- The impact of ionic liquid on protein structure and stability is poorly understood --- p.3
Chapter 1.2 --- PhAcP in [EMIM][BF₄] as a model to study the structure and stability of protein in ionic liquid by NMR spectroscopy --- p.6
Chapter 1.2.1 --- The application of [EMIM][BF₄] with protein --- p.6
Chapter 1.2.2 --- The background of PhAcP --- p.9
Chapter 1.2.3 --- Overview of the study --- p.10
Chapter Chapter 2 --- Materials and Methods --- p.12
Chapter 2.1 --- Expression and purification of PhAcP --- p.12
Chapter 2.1.1 --- Expression of PhAcP in Escherichia coli system --- p.12
Chapter 2.1.2 --- Purification of PhAcP --- p.14
Chapter 2.2 --- Solubility determination --- p.15
Chapter 2.3 --- NMR experiments --- p.17
Chapter 2.3.1 --- General procedures and sample preparation --- p.17
Chapter 2.3.2 --- ¹H-¹⁵N HSQC spectra in various concentrations of [EMIM][BF₄] --- p.18
Chapter 2.3.3 --- Structural characterization --- p.18
Chapter 2.3.4 --- Stability characterization --- p.19
Chapter Chapter 3 --- Results --- p.21
Chapter 3.1 --- Can the solubility of PhAcP in [EMIM][BF₄] reach the millimolar range required for NMR study? --- p.21
Chapter 3.2 --- Determination of the [EMIM][BF₄] concentration for a feasible NMR study --- p.23
Chapter 3.3 --- Backbone resonance assignment of PhAcP in 50% (v/v) [EMIM][BF₄] --- p.26
Chapter 3.4 --- Structural characterization of PhAcP in 50% (v/v) [EMIM][BF₄] --- p.29
Chapter 3.4.1 --- Secondary structure estimation by ¹³C secondary shifts --- p.29
Chapter 3.4.2 --- NOE connectivities within secondary structures --- p.35
Chapter 3.5 --- Characterization of the conformational stability of PhAcP in 50% (v/v) [EMIM][BF₄] by guanidine thiocyanate-induced denaturation --- p.40
Chapter Chapter 4 --- Discussion --- p.46
Chapter 4.1 --- The structure of PhAcP in 50% (v/v) [EMIM][BF₄] resembles the native conformation --- p.46
Chapter 4.2 --- The conformational stability of PhAcP has no observable change in 50% (v/v) [EMIM][BF₄] --- p.47
Chapter 4.3 --- Insight into the application of enzyme in ionic liquid --- p.48
Chapter 4.4 --- Limitation of the study --- p.49
Chapter 4.5 --- Insight into future studies --- p.50
Chapter Chapter 5 --- Conclusions --- p.51
Appendix --- p.53
References --- p.57
SOLDI, GEMMA. « Studies on the native-like aggregation of acylphosphatases ». Doctoral thesis, 2008. http://hdl.handle.net/2158/599244.
Texte intégralChapitres de livres sur le sujet "Acylphosphatase"
Nediani, Chiara, Gianfranco Liguri, Niccolò Taddei, Elena Marchetti, Giampietro Ramponi et Paolo Nassi. « Acylphosphatase and Calcium Transport Across Erythrocyte Membrane ». Dans Advances in Experimental Medicine and Biology, 207–15. Boston, MA : Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-5985-2_19.
Texte intégralLatorraca, S., C. Cecchi, A. Pieri, G. Liguri, L. Amaducci et S. Sorbi. « Acylphosphatase Levels In Alzheimer’s Disease Cultured Skin Fibroblasts ». Dans Advances in Behavioral Biology, 787–91. Boston, MA : Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5337-3_112.
Texte intégralWitzel, H., A. Billich, W. Berg, O. Creutzenberg et A. Karreh. « Nucleoside Phosphotransferase and Nuclease S1 Two Enzymes with Acylphosphate Intermediates, But Different Mechanisms ». Dans Metabolism and Enzymology of Nucleic Acids, 55–61. Boston, MA : Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-0749-5_7.
Texte intégral