Chaperonin ATPase
| 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 ADP + phosphate
These enzymes are a subclass of molecular chaperones.
References
- ↑ Hemmingsen, S.M.; Woolford, C.; van der Vies, S.M.; Tilly, K.; Dennis, D.T.; Georgopoulos, G.C.; Hendrix, R.W.; Ellis, R.J. (1988). "Homologous plant and bacterial proteins: chaperone oligomeric protein assembly". Nature. 333 (6171): 330–334. doi:10.1038/333330a0. PMID 2897629.
- ↑ Lubber, T.H.; Donaldson, G.K.; Viitanen, P.V.; Gatenby, A.A. (1989). "Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone". Plant Cell. 1 (12): 1223–1230. doi:10.1105/tpc.1.12.1223. PMID 2577724.
- ↑ Ellis, R.J., ed. (1996). The Chaperonins. San Diego: Academic Press. pp. –.
- ↑ Ranson, N.A.; White, H.E.; Saibil, H.R. (1998). "Chaperonins". Biochem. J. 333: 233–242. PMID 9657960.
See also
External links
- Chaperonin ATPase at the US National Library of Medicine Medical Subject Headings (MeSH)
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