KEGG   ENZYME: 3.6.4.10Help
Entry
EC 3.6.4.10                 Enzyme                                 

Name
non-chaperonin molecular chaperone ATPase;
molecular chaperone Hsc70 ATPase
Class
Hydrolases;
Acting on acid anhydrides;
Acting on acid anhydrides to facilitate cellular and subcellular movement
BRITE hierarchy
Sysname
ATP phosphohydrolase (polypeptide-polymerizing)
Reaction(IUBMB)
ATP + H2O = ADP + phosphate
Substrate
ATP [CPD:C00002];
H2O [CPD:C00001]
Product
ADP [CPD:C00008];
phosphate [CPD:C00009]
Comment
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.
History
EC 3.6.4.10 created 2000
Reference
1  [PMID:1356434]
  Authors
Sadis S, Hightower LE.
  Title
Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange.
  Journal
Biochemistry 31:9406-12 (1992)
Reference
2  [PMID:8509407]
  Authors
Blond-Elguindi S, Fourie AM, Sambrook JF, Gething MJ.
  Title
Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers.
  Journal
J Biol Chem 268:12730-5 (1993)
Reference
3  [PMID:7743994]
  Authors
Wawrzynow A, Wojtkowiak D, Marszalek J, Banecki B, Jonsen M, Graves B, Georgopoulos C, Zylicz M.
  Title
The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.
  Journal
EMBO J 14:1867-77 (1995)
Reference
4  [PMID:9083109]
  Authors
Sriram M, Osipiuk J, Freeman B, Morimoto R, Joachimiak A.
  Title
Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain.
  Journal
Structure 5:403-14 (1997)
DOI:10.1016/S0969-2126(97)00197-4
Reference
5  [PMID:9477575]
  Authors
Li X, Su RT, Hsu HT, Sze H.
  Title
The molecular chaperone calnexin associates with the vacuolar H(+)-ATPase from oat seedlings.
  Journal
Plant Cell 10:119-30 (1998)
Other DBs
ExplorEnz - The Enzyme Database: 3.6.4.10
IUBMB Enzyme Nomenclature: 3.6.4.10
ExPASy - ENZYME nomenclature database: 3.6.4.10
BRENDA, the Enzyme Database: 3.6.4.10

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