Biology:Non-chaperonin molecular chaperone ATPase
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Short description: Class of enzymes
| 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 | ||||||||
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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
References
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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
- Non-chaperonin+molecular+chaperone+ATPase at the US National Library of Medicine Medical Subject Headings (MeSH)
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