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J Biol Chem, Vol. 273, Issue 10, 5435-5438, March 6, 1998
From the Division of Enzyme Chemistry, Institute for Enzyme
Research, The University of Tokushima, Tokushima 770, Japan
Hsp70 is a multifunctional molecular chaperone
whose interactions with protein substrates are regulated by ATP
hydrolysis and ADP-ATP exchange. We show here that, in addition to
ATPase activity, purified Hsp70 free from nucleoside-diphosphate (NDP) kinase exhibits intrinsic ADP-ATP exchange activity. The rate constants
for ATP hydrolysis and ATP synthesis were in a similar range at the
optimum pH of 7.5-8.5 in the presence of 5 mM ATP and 0.5 mM ADP. Hsp70 exhibited a considerably strict
preference for ATP as a phosphate donor, and a biased substrate
specificity, unlike NDP kinase; ADP, UDP, CDP > dTDP, dCDP > GDP, dGDP. During the reaction, Hsp70 formed an acid-labile
autophosphorylated intermediate, and nucleoside diphosphate-dependent
dephosphorylation of the latter then occurred. These properties of
Hsp70 are not identical but similar to those of NDP kinase, but are not
similar to those of adenylate kinase and ATP synthase.
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