EC 3 - Hydrolases
EC 3.6 - Acting on acid anhydrides
EC 3.6.4 - Acting on ATP; involved in cellular and subcellular movement
EC 3.6.4.10 - Non-chaperonin molecular chaperone ATPase
IntEnz view
ENZYME view
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
- ATP + H2O = ADP + phosphate
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
References
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Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange.Biochemistry 31 : 9406-9412 (1992). [PMID: 1356434]
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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]
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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]
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Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain.Structure 5 : 403-414 (1997). [PMID: 9083109]
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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]