The Enzyme Database

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EC 3.6.4.10     
Accepted name: non-chaperonin molecular chaperone ATPase
Reaction: ATP + H2O = ADP + phosphate
Other name(s): molecular chaperone Hsc70 ATPase
Systematic name: ATP phosphohydrolase (polypeptide-polymerizing)
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: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sadis, S. and Hightower, L.E. Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry 31 (1992) 9406–9412. [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 (1993) 12730–12735. [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 (1995) 1867–1877. [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 (1997) 403–414. [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 (1998) 119–130. [PMID: 9477575]
[EC 3.6.4.10 created 2000]
 
 


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