Non-chaperonin molecular chaperone ATPase

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
Non-chaperonin molecular chaperone ATPase
Identifiers
EC number3.6.4.10
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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

See also

References

  1. Sadis S, Hightower LE (October 1992). "Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange". Biochemistry. 31 (39): 9406–12. doi:10.1021/bi00154a012. PMID 1356434.
  2. Blond-Elguindi S, Fourie AM, Sambrook JF, Gething MJ (June 1993). "Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers". The Journal of Biological Chemistry. 268 (17): 12730–5. PMID 8509407.
  3. Wawrzynow A, Wojtkowiak D, Marszalek J, Banecki B, Jonsen M, Graves B, Georgopoulos C, Zylicz M (May 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". The EMBO Journal. 14 (9): 1867–77. PMC 398286. PMID 7743994.
  4. Sriram M, Osipiuk J, Freeman B, Morimoto R, Joachimiak A (March 1997). "Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain". Structure. 5 (3): 403–14. doi:10.1016/s0969-2126(97)00197-4. PMID 9083109.
  5. Li X, Su RT, Hsu HT, Sze H (January 1998). "The molecular chaperone calnexin associates with the vacuolar H(+)-ATPase from oat seedlings". The Plant Cell. 10 (1): 119–30. doi:10.2307/3870633. PMC 143936. PMID 9477575.
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