The binding of ATP to the catalytic and the regulatory site of Ca2+, Mg2+-dependent ATPase of the sarcoplasmic reticulum.

Abstract:

:Two kinds of ATP binding sites were found on the ATPase molecule in deoxycholic acid-treated sarcoplasmic reticulum. One was the catalytic site (1 mol/mol active site) and its affinity was high. Upon addition of Ca2+, all the ATP bound to the catalytic site disappeared at 75 mM KCl, while a significant amount of ATP remained bound to the site at 0-2 mM KCl. The latter binding was found to be due to the formation of a slowly exchanging enzyme--ATP complex, which is in equilibrium with phosphoenzyme + ADP. The other binding site was the regulatory one (1 mol/mol active site) and its affinity was low, changing only insignificantly upon addition of Ca2+. The ATP binding to the regulatory site shifted the equilibrium between the slowly exchanging complex and EP toward EP.

journal_name

J Bioenerg Biomembr

authors

Nakamura Y,Tonomura Y

doi

10.1007/BF00743060

subject

Has Abstract

pub_date

1982-12-01 00:00:00

pages

307-18

issue

5-6

eissn

0145-479X

issn

1573-6881

journal_volume

14

pub_type

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