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A Product Inhibition Study on Adenosine Deaminase by Spectroscopy and Calorimetry
(Ali Akbar Saboury),(Ghasem Ataie Jafari),(Ali Akbar Moosavi Movahedi),(Mohammad Reza Housaindokht),(Gholam Hosain Hakimelahi),(Adeleh Divsalar) 생화학분자생물학회 2002 BMB Reports Vol.35 No.3
Kinetic and thermodynamic studies have been made on the effect of the inosine product on the activity of adenosine deaminase in a 50 mM sodium phosphate buffer, pH 7.5, at 27oC using UV spectrophotometry and isothermal titration calorimetry (ITC). A competitive inhibition was observed for inosine as a product of the enzymatic reaction. A graphical-fitting method was used for determination of the binding constant and enthalpy of inhibitor binding by using isothermal titration microcalorimetry data. The dissociation-binding constant is equal to 140 μM by the microcalorimetry method, which agrees well with the value of 143 μM for the inhibition constant that was obtained from the spectroscopy method.
A Product Inhibition Study on Adenosine Deaminase by Spectroscopy and Calorimetry
Saboury, Ali Akbar,Divsalar, Adeleh,Jafari, Ghasem Ataie,Moosavi-Movahedi, Ali Akbar,Housaindokht, Mohammad Reza,Hakimelahi, Hosain 생화학분자생물학회 2002 Journal of biochemistry and molecular biology Vol.35 No.3
Kinetic and thermodynamic studies have been made on the effect of the inosine product on the activity of adenosine deaminase in a 50 mM sodium phosphate buffer, pH 7.5, at $27^{\circ}C$ using UV spectrophotometry and isothermal titration calorimetry (ITC). A competitive inhibition was observed for inosine as a product of the enzymatic reaction. A graphical-fitting method was used for determination of the binding constant and enthalpy of inhibitor binding by using isothermal titration microcalorimetry data. The dissociation-binding constant is equal to $140\;{\mu}M$ by the microcalorimetry method, which agrees well with the value of $143\;{\mu}M$ for the inhibition constant that was obtained from the spectroscopy method.
Davood Ajloo,Leila Najafi,Ali Akbar Saboury 대한화학회 2009 Bulletin of the Korean Chemical Society Vol.30 No.11
Effects of some diacid, diamine and dinitro aromatic compounds on the structure and activity of adenosine deaminase (ADA) were investigated by UV-Vis spectrophotometry in 50 mM phosphate buffer at pH = 7.5 and 27°C and molecular docking studies. The results showed that all tested ligands are showing inhibition; five ligands are uncompetitive and other two ligands are mixed of competitive and noncompetetive inhibitors with majority of competitive behavior. For the later case analysis was done based on competitive inhibition. Diacids have larger size and higher inhibition constant (KI) relative to others. A logical correlation between calculated free energy of binding and experimental values was obtained for un-competitive. Experimental and calculated data showed that competitive inhibitors are distributed near the active site of enzyme and form several cluster of ranks, whereas uncompetitive inhibitors bind to the enzyme-substrate complex and distributed far from the active site. Results of structure-activity relationship showed that, larger, more hydrophobe, less spherical and more aromatic ligands have higher inhibition constants.
Effect of Cationic and Anionic Porphyrins on the Structure and Activity of Adenosine Deaminase
Ajloo, Davood,Hajipour, Samaneh,Saboury, Ali Akbar,Zakavi, Saeed Korean Chemical Society 2011 Bulletin of the Korean Chemical Society Vol.32 No.9
Kinetic and structural studies have been carried out on the effects of meso-tetrakis(4-sulfonatophenyl)-porphyrin ($H_2TPPS_4$) as an anionic and meso-tetrakis(3-N-methyl-pyridyl)porphyrin ($H_2TMPYP$) as a cationic porphyrin with adenosine deaminase (ADA) in 25 mM citrate/phosphate buffer, pH = 4-8, at $37^{\circ}C$ using UVvis spectrophotometry, circular dichroism (CD), fluorescence spectrophotometry as well as molecular dynamics (MD) and molecular docking. Kinetic results showed that the two porphyrins are non-competitive inhibitors. Increasing pH, increases $K_I$ and cationic porphyrin has a higher $K_I$ and lower binding constant ($K_b$) at all pH ranges. Analyzing the secondary structure revealed that both ligands decrease the secondary structure and that the anionic porphyrin is more effective.
Ajloo, Davood,Najafi, Leila,Saboury, Ali Akbar Korean Chemical Society 2009 Bulletin of the Korean Chemical Society Vol.30 No.11
Effects of some diacid, diamine and dinitro aromatic compounds on the structure and activity of adenosine deaminase (ADA) were investigated by UV-Vis spectrophotometry in 50 mM phosphate buffer at pH = 7.5 and 27 ${^{\circ}C}$ and molecular docking studies. The results showed that all tested ligands are showing inhibition; five ligands are uncompetitive and other two ligands are mixed of competitive and noncompetetive inhibitors with majority of competitive behavior. For the later case analysis was done based on competitive inhibition. Diacids have larger size and higher inhibition constant ($K_I$) relative to others. A logical correlation between calculated free energy of binding and experimental values was obtained for un-competitive. Experimental and calculated data showed that competitive inhibitors are distributed near the active site of enzyme and form several cluster of ranks, whereas uncompetitive inhibitors bind to the enzyme-substrate complex and distributed far from the active site. Results of structure-activity relationship showed that, larger, more hydrophobe, less spherical and more aromatic ligands have higher inhibition constants.
Effect of Cationic and Anionic Porphyrins on the Structure and Activity of Adenosine Deaminase
Davood Ajloo,Samaneh Hajipour,Ali Akbar Saboury,Saeed Zakavi 대한화학회 2011 Bulletin of the Korean Chemical Society Vol.32 No.9
Kinetic and structural studies have been carried out on the effects of meso-tetrakis(4-sulfonatophenyl)-porphyrin (H_2TPPS_4) as an anionic and meso-tetrakis(3-N-methyl-pyridyl)porphyrin (H_2TMPYP) as a cationic porphyrin with adenosine deaminase (ADA) in 25 mM citrate/phosphate buffer, pH = 4-8, at 37 ^oC using UVvis spectrophotometry, circular dichroism (CD), fluorescence spectrophotometry as well as molecular dynamics (MD) and molecular docking. Kinetic results showed that the two porphyrins are non-competitive inhibitors. Increasing pH, increases K_I and cationic porphyrin has a higher K_I and lower binding constant (K_b)at all pH ranges. Analyzing the secondary structure revealed that both ligands decrease the secondary structure and that the anionic porphyrin is more effective.
Yousefi, Reza,Ardestani, Susan K.,Saboury, Ali Akbar,Kariminia, Amina,Zeinali, Madjid,Amani, Mojtaba Korean Society for Biochemistry and Molecular Biol 2005 Journal of biochemistry and molecular biology Vol.38 No.4
Calcium and zinc binding protein, calprotectin is a multifunctional protein with broad spectrum antimicrobial and antitumoural activity. It was purified from human neutrophil, using a two-step ion exchange chromatography. Since surface hydrophobicity of calprotectin may be important in membrane anchoring, membrane penetration, subunits oligomerization and some biological roles of protein, in this study attempted to explore the effect of calcium in physiological range on the calprotectin lipophilicity. Incubation of human calprotectin ($50\;{\mu}g/ml$) with different calcium concentrations showed that 1-anilino-8-naphthalene sulfonic acid (ANS) fluorescence intensity of the protein significantly elevates with calcium in a dose dependent manner, suggesting an increase in calprotectin surface hydrophobicity upon calcium binding. Our study also indicates that calcium at higher concentrations (6, 8 and 10 mM) induces aggregation of human calprotectin. Our finding demonstrates that the starting time and the rate constant of calprotectin aggregation depend on the calcium concentration.