KEGG   ENZYME: 3.6.4.9Help
Entry
EC 3.6.4.9                  Enzyme                                 

Name
chaperonin ATPase;
chaperonin
Class
Hydrolases;
Acting on acid anhydrides;
Acting on acid anhydrides to facilitate cellular and subcellular movement
BRITE hierarchy
Sysname
ATP phosphohydrolase (polypeptide-unfolding)
Reaction(IUBMB)
ATP + H2O = ADP + phosphate [RN:R00086]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
H2O [CPD:C00001]
Product
ADP [CPD:C00008];
phosphate [CPD:C00009]
Comment
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).
History
EC 3.6.4.9 created 2000
Reference
1  [PMID:2897629]
  Authors
Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ.
  Title
Homologous plant and bacterial proteins chaperone oligomeric protein assembly.
  Journal
Nature. 333 (1988) 330-4.
  Organism
Escherichia coli
Reference
2  [PMID:2577724]
  Authors
Lubben TH, Donaldson GK, Viitanen PV, Gatenby AA
  Title
Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone.
  Journal
Plant. Cell. 1 (1989) 1223-30.
Reference
3
  Authors
In: Ellis, R.J. (Ed.), The Chaperonins, Academic Press, San Diego, 1996.
Reference
4  [PMID:9657960]
  Authors
Ranson NA, White HE, Saibil HR.
  Title
Chaperonins.
  Journal
Biochem. J. 333 ( Pt 2) (1998) 233-42.
  Organism
Escherichia coli
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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