EC 3.6.4.10 - Non-chaperonin molecular chaperone ATPase

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IntEnz Enzyme Nomenclature
EC 3.6.4.10

Names

Accepted name:
non-chaperonin molecular chaperone ATPase
Other name:
molecular chaperone Hsc70 ATPase
Systematic name:
ATP phosphohydrolase (polypeptide-polymerizing)

Reaction

Comments:

This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00269
Structural data: CSA , EC2PDB

References

  1. Sadis, S. and Hightower, L.E.
    Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange.
    Biochemistry 31: 9406-9412 (1992). [PMID: 1356434]
  2. Blond-Elquindi, S., Fourie, A.M., Sambrook, J.F. and Gething, M.J.
    Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers.
    J. Biol. Chem. 268: 12730-12735 (1993). [PMID: 8509407]
  3. Wawrzynow, A., Wojtkowiak, D., Marszalek, J., Banecki, B., Jonsen, M., Graves, B., Georgopoulos, C. and Zylicz, M.
    The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.
    EMBO J. 14: 1867-1877 (1995). [PMID: 7743994]
  4. Sriram, M., Osipiuk, J., Freeman, B., Morimoto, R. and Joachimiak, A.
    Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain.
    Structure 5: 403-414 (1997). [PMID: 9083109]
  5. Li, X., Su, R.T., Hsu, H.T. and Sze, H.
    The molecular chaperone calnexin associated with the vacuolar H+-ATPase from oat seedlings.
    Plant Cell 10: 119-130 (1998). [PMID: 9477575]

[EC 3.6.4.10 created 2000]