Chaperonin ATPase
| Chaperonin ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 ADP + phosphate
These enzymes are a subclass of molecular chaperones.
See also
[edit]References
[edit]- ^ Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ (May 1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature. 333 (6171): 330–4. doi:10.1038/333330a0. PMID 2897629.
- ^ Lubben TH, Donaldson GK, Viitanen PV, Gatenby AA (December 1989). "Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone". The Plant Cell. 1 (12): 1223–30. doi:10.1105/tpc.1.12.1223. PMC 159857. PMID 2577724.
- ^ Ellis, R.J., ed. (1996). The Chaperonins. San Diego: Academic Press. pp. -.
- ^ Ranson NA, White HE, Saibil HR (July 1998). "Chaperonins". The Biochemical Journal. 333 ( Pt 2): 233–42. PMC 1219577. PMID 9657960.
External links
[edit]- Chaperonin+ATPase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
