EC 3.6.4.9 - Chaperonin ATPase

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IntEnz Enzyme Nomenclature
EC 3.6.4.9

Names

Accepted name:
chaperonin ATPase
Other name:
chaperonin
Systematic name:
ATP phosphohydrolase (polypeptide-unfolding)

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

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: 330-334 (1988). [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: 1223-1230 (1989).
  3. In: 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: 233-242 (1998). [PMID: 9657960]

[EC 3.6.4.9 created 2000]