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

Non-chaperonin molecular chaperone ATPase
Identifiers
EC no.3.6.4.10
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins
ATP + H2O ADP + phosphate

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

See also

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References

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  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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