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 \rightleftharpoons ADP + phosphate

These enzymes are a subclass of molecular chaperones.

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. (1988). "Homologous plant and bacterial proteins: chaperone oligomeric protein assembly". Nature 333 (6171): 330–334. doi:10.1038/333330a0. PMID 2897629.
  2. Lubber, T.H., Donaldson, G.K., Viitanen, P.V. and 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.
  3. Ellis, R.J., ed. (1996). The Chaperonins. San Diego: Academic Press. pp. –.
  4. Ranson, N.A., White, H.E. and Saibil, H.R. (1998). "Chaperonins". Biochem. J. 333: 233–242. PMID 9657960.

See also

External links

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