Home  |  Contact

ENZYME entry: EC 5.6.1.7

Accepted Name
Chaperonin ATPase.
Alternative Name(s)
Chaperonin.
Reaction catalysed
ATP + H(2)O + a folded polypeptide <=> ADP + phosphate + an unfolded polypeptide
Comment(s)
  • 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.
  • Formerly EC 3.6.4.9.
Cross-references
BRENDA5.6.1.7
EC2PDB5.6.1.7
ExplorEnz5.6.1.7
PRIAM enzyme-specific profiles5.6.1.7
KEGG Ligand Database for Enzyme Nomenclature5.6.1.7
IUBMB Enzyme Nomenclature5.6.1.7
IntEnz5.6.1.7
MEDLINEFind literature relating to 5.6.1.7
MetaCyc5.6.1.7
UniProtKB/Swiss-Prot
P31081, CH60_BOVIN;  P49818, CH60_CANLF;  Q5ZL72, CH60_CHICK;  
P18687, CH60_CRIGR;  P10809, CH60_HUMAN;  P86206, CH60_MESAU;  
P63038, CH60_MOUSE;  Q5NVM5, CH60_PONAB;  P63039, CH60_RAT;  

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 5.6.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 5.6.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 5.-.-.-