KEGG   ENZYME: 5.6.1.7
Entry
EC 5.6.1.7                  Enzyme                                 

Name
chaperonin ATPase;
chaperonin
Class
Isomerases;
Isomerases altering macromolecular conformation;
Enzymes altering polypeptide conformation or assembly
Sysname
ATP phosphohydrolase (polypeptide-unfolding)
Reaction(IUBMB)
ATP + H2O + an unfolded polypeptide = ADP + phosphate + a folded polypeptide
Substrate
ATP [CPD:C00002];
H2O [CPD:C00001];
unfolded polypeptide
Product
ADP [CPD:C00008];
phosphate [CPD:C00009];
folded polypeptide
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 5.6.1.5 (proteasome ATPase).
History
EC 5.6.1.7 created 2000 as EC 3.6.4.9, transferred 2018 to EC 5.6.1.7
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 333:330-4 (1988)
DOI:10.1038/333330a0
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 1:1223-30 (1989)
DOI:10.1105/tpc.1.12.1223
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):233-42 (1998)
DOI:10.1042/bj3330233
Other DBs
ExplorEnz - The Enzyme Database: 5.6.1.7
IUBMB Enzyme Nomenclature: 5.6.1.7
ExPASy - ENZYME nomenclature database: 5.6.1.7
BRENDA, the Enzyme Database: 5.6.1.7

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