Article
Regulation of heat shock protein 90 ATPase activity by sequences in the carboxyl terminus.
The Journal of biological chemistry - 1 Mar 2002
Owen Barbara A L, Sullivan William P, Felts Sara J, Toft David O
Abstract excerpt
Hsp90, in addition to being an abundant and pivotal cytoplasmic chaperone protein, has been shown to be a weak ATPase. In an effort to characterize the ATPase activity of hsp90, we have observed marked differences in activities among various species of hsp90. Chicken or human hsp90 hydrolyzed ATP with a k(cat) of 0.02 min(-1) and a K(m) greater than 300 microm. In contrast, yeast hsp90 and TRAP1, an hsp90...
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