Biology:Non-chaperonin molecular chaperone ATPase

From HandWiki
Short description: Class of enzymes
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

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 [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate

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

See also

References

  1. "Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange". Biochemistry 31 (39): 9406–12. October 1992. doi:10.1021/bi00154a012. PMID 1356434. 
  2. "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. June 1993. PMID 8509407. 
  3. "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. May 1995. PMID 7743994. 
  4. "Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain". Structure 5 (3): 403–14. March 1997. doi:10.1016/s0969-2126(97)00197-4. PMID 9083109. 
  5. "The molecular chaperone calnexin associates with the vacuolar H(+)-ATPase from oat seedlings". The Plant Cell 10 (1): 119–30. January 1998. doi:10.2307/3870633. PMID 9477575. 

External links