Molekulski šaperon Hsc70 ATPaza

Šaperon (protein)
Identifikatori
EC broj 3.6.4.10
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum

Šaperon (protein) (EC 3.6.4.10, molekulski šaperon Hsc70 ATPaza) je enzim sa sistematskim imenom ATP fosfohidrolaza (polimerizacija polipeptida).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

ATP + H2O ADP + fosfat

Ova veoma raznovrsna grupa enzima vrši mnoštvo funkcija koje su slične sa funkcijama šaperonina.

Reference

  1. ↑ Sadis, S. and Hightower, L.E. (1992). „Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange”. Biochemistry 31: 9406-9412. PMID 1356434. 
  2. ↑ Blond-Elquindi, S., Fourie, A.M., Sambrook, J.F. and 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. and 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. PMID 7743994. 
  4. ↑ Sriram, M., Osipiuk, J., Freeman, B., Morimoto, R. and Joachimiak, A. (1997). „Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain”. Structure 5: 403-414. PMID 9083109. 
  5. ↑ Li, X., Su, R.T., Hsu, H.T. and Sze, H. (1998). „The molecular chaperone calnexin associated with the vacuolar H+-ATPase from oat seedlings”. Plant Cell 10: 119-130. PMID 9477575. 

Literatura

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