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Information on EC 5.6.1.7 - chaperonin ATPase

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EC Tree
IUBMB Comments
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).
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
a folded polypeptide
=
+
+
an unfolded polypeptide
Synonyms
chaperonin, hsp65, groes, heat shock protein 60, cpn60, hsp10, cpn10, chaperonin groel, chaperonin 60, groel2, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
show the reaction diagram
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