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Non-chaperonin molecular chaperone ATPase
Class of enzymes
Class of enzymes
| Field | Value |
|---|---|
| Name | Non-chaperonin molecular chaperone ATPase |
| EC_number | 3.6.4.10 |
Non-chaperonin molecular chaperone ATPase (, molecular chaperone Hsc70 ATPase) is an enzyme with systematic name ATP phosphohydrolase (polypeptide-polymerizing). This enzyme catalyses the following chemical reaction
: ATP + H2O \rightleftharpoons ADP + phosphate
These enzymes perform many functions that are similar to those of chaperonins.
References
References
- (October 1992). "Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange". Biochemistry.
- (June 1993). "Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers". The Journal of Biological Chemistry.
- (May 1995). "The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone". The EMBO Journal.
- (March 1997). "Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain". Structure.
- (January 1998). "The molecular chaperone calnexin associates with the vacuolar H(+)-ATPase from oat seedlings". The Plant Cell.
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