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Non-chaperonin molecular chaperone ATPase

Class of enzymes


Class of enzymes

FieldValue
NameNon-chaperonin molecular chaperone ATPase
EC_number3.6.4.10

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

  1. (October 1992). "Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange". Biochemistry.
  2. (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.
  3. (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.
  4. (March 1997). "Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain". Structure.
  5. (January 1998). "The molecular chaperone calnexin associates with the vacuolar H(+)-ATPase from oat seedlings". The Plant Cell.
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