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. 1981 Feb;78(2):761–765. doi: 10.1073/pnas.78.2.761

Activation of the heat-stable polypeptide of the ATP-dependent proteolytic system.

A Ciechanover, H Heller, R Katz-Etzion, A Hershko
PMCID: PMC319882  PMID: 6262770

Abstract

It had been shown previously that the heat-stable polypeptide of the ATP-dependent proteolytic system of reticulocytes, designated APF-1, forms covalent conjugates with protein substrates in an ATP-requiring process. We now describe an enzyme that carries out the activation by ATP of the polypeptide with pyrophosphate displacement. The formation of AMP-polypeptide and transfer of the polypeptide to a secondary acceptor are suggested by an APF-1 requirement for ATP-PPi and ATP-AMP exchange reactions, respectively. With radiolabeled polypeptide, an ATP-dependent labeling of the enzyme was shown to be by a linkage that is acid stable but is labile to treatment with mild alkali, hydroxylamine, borohydride, or mercuric salts. It therefore appears that the AMP-polypeptide undergoes attack by an -SH group of the enzyme to form a thiolester.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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