ExplorEnz: EC 5.6.1.7

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5.6.1.7

Accepted name:

chaperonin ATPase

Reaction:

ATP + H₂O + an unfolded polypeptide = ADP + phosphate + a folded polypeptide

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 5.6.1.5 (proteasome ATPase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

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. [DOI] [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. [DOI] [PMID: 2577724]
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 5.6.1.7 created 2000 as EC 3.6.4.9, transferred 2018 to EC 5.6.1.7]