Biology:Chaperonin ATPase
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Short description: Class of enzymes
| Chaperonin ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.4.9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Chaperonin ATPase (EC 3.6.4.9, chaperonin) is an enzyme with systematic name ATP phosphohydrolase (polypeptide-unfolding).[1][2][3][4] This enzyme catalyses the following chemical reaction
- ATP + H2O [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate
These enzymes are a subclass of molecular chaperones.
See also
References
- ↑ "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature 333 (6171): 330–4. May 1988. doi:10.1038/333330a0. PMID 2897629.
- ↑ "Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone". The Plant Cell 1 (12): 1223–30. December 1989. doi:10.1105/tpc.1.12.1223. PMID 2577724.
- ↑ Ellis, R.J., ed (1996). The Chaperonins. San Diego: Academic Press. pp. -.
- ↑ "Chaperonins". The Biochemical Journal 333 ( Pt 2): 233–42. July 1998. PMID 9657960.
External links
- Chaperonin+ATPase at the US National Library of Medicine Medical Subject Headings (MeSH)
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