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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Published in | Moscow University chemistry bulletin Vol. 75; no. 6; pp. 374 - 381 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Moscow
Pleiades Publishing
01.11.2020
Springer Nature B.V |
Subjects | |
Online Access | Get full text |
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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. |
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ISSN: | 0027-1314 1935-0260 |
DOI: | 10.3103/S0027131420060139 |