IUBMB Enzyme Nomenclature

EC 3.6.4.9

Accepted name: chaperonin ATPase

Reaction: ATP + H2O = ADP + phosphate

Other name(s): chaperonin

Systematic name: ATP phosphohydrolase (polypeptide-unfolding)

Comments: Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa. They are a subclass of molecular chaperones that are related to EC 3.6.4.8 (proteasome ATPase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Hemmingsen, S.M., Woolford, C., van der Vies, S.M., Tilly, K., Dennis, D.T., Georgopoulos, G.C., Hendrix, R.W. and Ellis, R.J. Homologous plant and bacterial proteins: chaperone oligomeric protein assembly. Nature 333 (1988) 330-334. [PMID: 2897629]

2. Lubber, T.H., Donaldson, G.K., Viitanen, P.V. and Gatenby, A.A. Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone. Plant Cell 1 (1989) 1223-1230.

3. Ellis, R.J. (Ed.), The Chaperonins, Academic Press, San Diego, 1996.

4. Ranson, N.A., White, H.E. and Saibil, H.R. Chaperonins. Biochem. J. 333 (1998) 233-242. [PMID: 9657960]

[EC 3.6.4.9 created 2000]


Return to EC 3.6.4 home page
Return to EC 3.6 home page
Return to EC 3 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page