Non-chaperonin molecular chaperone ATPase

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Non-chaperonin molecular chaperone ATPase
Identifiers
EC number 3.6.4.10
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Non-chaperonin molecular chaperone ATPase (EC 3.6.4.10, 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]

References[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. 

External links[edit]