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Article

Modulatory ATP binding affinity in intermediate states of E2P dephosphorylation of sarcoplasmic reticulum Ca2+-ATPase.

The Journal of biological chemistry - 1 Apr 2011

Clausen Johannes D, McIntosh David B, Woolley David G, Andersen Jens Peter

Abstract excerpt

The mechanism of ATP modulation of E2P dephosphorylation of sarcoplasmic reticulum Ca(2+)-ATPase wild type and mutant forms was examined in nucleotide binding studies of states analogous to the various intermediates of the dephosphorylation reaction, obtained by binding of metal fluorides, vanadate, or thapsigargin. Wild type Ca(2+)-ATPase displays an ATP affinity of 4 μM for the E2P ground state analog, 1 μM for...

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Identifiers

PMID: 21288896
DOI: 10.1074/jbc.M110.206094
PMCID: PMC3064230

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Source receipt: pubmed, retrieved 7 Sept 2026.

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