IntEnz

EC 3.6.4.10 - Non-chaperonin molecular chaperone ATPase

IntEnz Enzyme Nomenclature
EC 3.6.4.10

Names

Reaction

• 13065 [IUBMB]
  ATP

  ATP

  Name origin: UniProt - CHECKED (C)

  CHEBI:30616

  Formula: C10H12N5O13P3
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  ADP

  ADP

  Name origin: UniProt - CHECKED (C)

  CHEBI:456216

  Formula: C10H12N5O10P2
  Charge: -3

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  phosphate

  phosphate

  Name origin: UniProt - CHECKED (C)

  CHEBI:43474

  Formula: HO4P
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

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

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]