Binding of intrinsic ATPase inhibitor to mitochondrial ATPase--stoichiometry of binding of nucleotides, inhibitor, and enzyme.

Abstract:

:F1-ATPase inhibitor was purified from yeast, Saccharomyces cerevisiae. The purified inhibitor blocked ATPase activity in the presence of ATP and Mg2+ by forming a latent equimolar enzyme-inhibitor complex with ATP and ADP newly bound to loose sites on the enzyme. A small portion of externally added ATP was hydrolyzed before the latent complex was formed but the hydrolysis was not directly related to the complex formation. Newly bound ATP tended to be converted to ADP when the ATP concentration of the medium was low. ATP tightly bound to the enzyme was not directly involved in formation of the complex. The complex was fairly stable in the presence of excess inhibitor and ATP but at a high concentration of the enzyme (10(-5) M), the inhibition was not complete, although only about 0.03% of the original activity remained unblocked.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Hashimoto T,Negawa Y,Tagawa K

doi

10.1093/oxfordjournals.jbchem.a133567

subject

Has Abstract

pub_date

1981-10-01 00:00:00

pages

1151-7

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

90

pub_type

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