Chaperonin ATPase

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Chaperonin ATPase
Identifiers
EC no.3.6.4.9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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.

See also[]

References[]

  1. ^ Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ (May 1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature. 333 (6171): 330–4. doi:10.1038/333330a0. PMID 2897629.
  2. ^ Lubben TH, Donaldson GK, Viitanen PV, Gatenby AA (December 1989). "Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone". The Plant Cell. 1 (12): 1223–30. doi:10.1105/tpc.1.12.1223. PMC 159857. PMID 2577724.
  3. ^ Ellis, R.J., ed. (1996). The Chaperonins. San Diego: Academic Press. pp. -.
  4. ^ Ranson NA, White HE, Saibil HR (July 1998). "Chaperonins". The Biochemical Journal. 333 ( Pt 2): 233–42. PMC 1219577. PMID 9657960.

External links[]

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