Studies on inorganic pyrophosphatase using imidodiphosphate as a substrate

Baker's yeast inorganic pyrophosphatase has been found to catalyze Mg 2+-dependent hydrolysis of imidodiphosphate yielding phosphate and amidophosphate. The reaction proceeds linearly in the presteady state. The catalytic constant is maximal at pH 9.0 and equals 0.5 min −1. Kinetic titrations o...

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Bibliographic Details
Published inFEBS letters Vol. 206; no. 1; pp. 121 - 124
Main Authors Smirnova, Irina N., Baykov, Alexander A., Avaeva, Svetlana M.
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 29.09.1986
Elsevier
Subjects
Active-site titration
Analytical, structural and metabolic biochemistry
Binding Sites
Biological and medical sciences
Diphosphonates - metabolism
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Hydrolases
Imidodiphosphate
Inorganic pyrophosphatase
Kinetics
Magnesium - metabolism
Magnesium - pharmacology
Metal-ion cofactor
Phosphates - metabolism
PNP
Pyrophosphatases - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Metal-ion cofactor
Inorganic pyrophosphatase
PNP
Imidodiphosphate
Active-site titration
Yeast
Enzyme
Substrate analog
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Summary:Baker's yeast inorganic pyrophosphatase has been found to catalyze Mg 2+-dependent hydrolysis of imidodiphosphate yielding phosphate and amidophosphate. The reaction proceeds linearly in the presteady state. The catalytic constant is maximal at pH 9.0 and equals 0.5 min −1. Kinetic titrations of the enzyme with imidodiphosphate and Mg 2+ have provided direct evidence for the involvement of three Mg 2+ per active site in the transition state of the pyrophosphatase reaction.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(86)81352-7