The Kinetics of Hydrolysis of ATP by Apyrase A from Solanum tuberosum

The kinetics of the hydrolysis of ATP by apyrase A from the Solanum tuberosum potato is studied at a pH of 6.5 and 25°C by the bioluminescent method. K M = 33 μM and V = 0.37 μM/s are determined for ATP. It is shown that the hydrolysis of ATP proceeds in two stages. The fast and slow stages of the r...

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Bibliographic Details
Published inMoscow University chemistry bulletin Vol. 75; no. 6; pp. 374 - 381
Main Authors Lomakina, G. Yu, Konik, P. A., Ugarova, N. N.
Format Journal Article
LanguageEnglish
Published Moscow Pleiades Publishing 01.11.2020
Springer Nature B.V
Subjects
Catalytic activity
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Hydrolysis
Kinetics
Potatoes
adenosine-5'-triphosphate
adenosine-5'-diphosphate
apyrase A
ATP
ADP
bioluminescent analysis
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Summary:The kinetics of the hydrolysis of ATP by apyrase A from the Solanum tuberosum potato is studied at a pH of 6.5 and 25°C by the bioluminescent method. K M = 33 μM and V = 0.37 μM/s are determined for ATP. It is shown that the hydrolysis of ATP proceeds in two stages. The fast and slow stages of the reaction are described by pseudo-first-order exponents. According to the hypothesis proposed, the intermediate complex of apyrase with ADP which is formed at the fast stage of the reaction possesses catalytic activity in the hydrolysis reaction of ATP but it is lower compared to free apyrase. This complex hydrolyzes ATP at the slow stage of the reaction.
ISSN:0027-1314
1935-0260
DOI:10.3103/S0027131420060139