Non-chaperonin molecular chaperone ATPase

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Non-chaperonin molecular chaperone ATPase
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Non-chaperonin molecular chaperone ATPase (EC, molecular chaperone Hsc70 ATPase) is an enzyme with systematic name ATP phosphohydrolase (polypeptide-polymerizing).[1][2][3][4][5] This enzyme catalyses the following chemical reaction

ATP + H2O ADP + phosphate

These enzymes perform many functions that are similar to those of chaperonins.

See also[edit]


  1. ^ Sadis, S.; Hightower, L.E. (1992). "Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange". Biochemistry. 31: 9406–9412. doi:10.1021/bi00154a012. PMID 1356434. 
  2. ^ Blond-Elquindi, S.; Fourie, A.M.; Sambrook, J.F.; Gething, M.J. (1993). "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. PMID 8509407. 
  3. ^ Wawrzynow, A.; Wojtkowiak, D.; Marszalek, J.; Banecki, B.; Jonsen, M.; Graves, B.; Georgopoulos, C.; Zylicz, M. (1995). "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. PMC 398286Freely accessible. PMID 7743994. 
  4. ^ Sriram, M.; Osipiuk, J.; Freeman, B.; Morimoto, R.; Joachimiak, A. (1997). "Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain". Structure. 5: 403–414. doi:10.1016/s0969-2126(97)00197-4. PMID 9083109. 
  5. ^ Li, X.; Su, R.T.; Hsu, H.T.; Sze, H. (1998). "The molecular chaperone calnexin associated with the vacuolar H+-ATPase from oat seedlings". Plant Cell. 10: 119–130. doi:10.2307/3870633. PMC 143936Freely accessible. PMID 9477575. 

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