Inhibition of β-Amylase Activity by Calcium, Magnesium and Zinc Ions Determined by Spectrophotometry and Isothermal Titration Calorimetry

The inhibition effect of metal ions on beta amylase activity was studied. The inhibitor-binding constant (Ki) was determined by spectrophotometric and isothermal titration calorimetric (ITC) methods. The binding of calcium, magnesium and zinc ion as inhibitors at the active site of barley beta amyla...

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Published inJournal of enzyme inhibition and medicinal chemistry Vol. 19; no. 2; pp. 157 - 160
Main Authors Umar Dahot, M., Saboury, A.A., Moosavi-Movahedi, A.A.
Format Journal Article
LanguageEnglish
Published England Taylor & Francis 01.04.2004
Subjects
beta-Amylase - antagonists & inhibitors
Calcium - pharmacology
Calorimetry - methods
Cations, Divalent
Inhibition
Isothermal titration calorimetry
Kinetics
Magnesium - pharmacology
Metal ions
Spectrophotometry
Zinc - pharmacology
β-Amylase
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Abstract The inhibition effect of metal ions on beta amylase activity was studied. The inhibitor-binding constant (Ki) was determined by spectrophotometric and isothermal titration calorimetric (ITC) methods. The binding of calcium, magnesium and zinc ion as inhibitors at the active site of barley beta amylase was studied at pH=4.8 (sodium acetate 16 mM) and T=300 K. The Ki and enthalpy of binding for calcium (13.4, 13.1 mM and -14.3 kJ/mol), magnesium (18.6, 17.8 mM and -17.7 kJ/mol) and zinc (17.5, 17.7 mM and -20.0 kJ/mol) were found by spectrophotometric and ITC methods respectively.
AbstractList The inhibition effect of metal ions on beta amylase activity was studied. The inhibitor-binding constant (Ki) was determined by spectrophotometric and isothermal titration calorimetric (ITC) methods. The binding of calcium, magnesium and zinc ion as inhibitors at the active site of barley beta amylase was studied at pH = 4.8 (sodium acetate 16 mM) and T = 300K. The Ki and enthalpy of binding for calcium (13.4, 13.1 mM and -14.3 kJ/mol), magnesium (18.6, 17.8mM and -17.7 kJ/mol) and zinc (17.5, 17.7 mM and -20.0 kJ/mol) were found by spectrophotometric and ITC methods respectively.
The inhibition effect of metal ions on beta amylase activity was studied. The inhibitor-binding constant (Ki) was determined by spectrophotometric and isothermal titration calorimetric (ITC) methods. The binding of calcium, magnesium and zinc ion as inhibitors at the active site of barley beta amylase was studied at pH=4.8 (sodium acetate 16 mM) and T=300 K. The Ki and enthalpy of binding for calcium (13.4, 13.1 mM and -14.3 kJ/mol), magnesium (18.6, 17.8 mM and -17.7 kJ/mol) and zinc (17.5, 17.7 mM and -20.0 kJ/mol) were found by spectrophotometric and ITC methods respectively.
Author Umar Dahot, M.
Moosavi-Movahedi, A.A.
Saboury, A.A.
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10.3109/14756369709035819
10.1021/cr960436q
10.1002/j.2050-0416.1996.tb00912.x
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Snippet The inhibition effect of metal ions on beta amylase activity was studied. The inhibitor-binding constant (Ki) was determined by spectrophotometric and...
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SubjectTerms beta-Amylase - antagonists & inhibitors
Calcium - pharmacology
Calorimetry - methods
Cations, Divalent
Inhibition
Isothermal titration calorimetry
Kinetics
Magnesium - pharmacology
Metal ions
Spectrophotometry
Zinc - pharmacology
β-Amylase
Title Inhibition of β-Amylase Activity by Calcium, Magnesium and Zinc Ions Determined by Spectrophotometry and Isothermal Titration Calorimetry
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Volume 19
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