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Literature summary extracted from

  • Figueiredo, L.; Klunker, D.; Ang, D.; Naylor, D.J.; Kerner, M.J.; Georgopoulos, C.; Hartl, F.U.; Hayer-Hartl, M.
    Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation (2004), J. Biol. Chem., 279, 1090-1099.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.6.1.7 ammonium sulfate optimal functionality of MmGroEL/GroES and its ability to encapsulate larger proteins, such as malate dehydrogenase, requires the presence of ammonium sulfate in vitro Methanosarcina mazei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.6.1.7 ATP + H2O + a folded polypeptide Methanosarcina mazei the archaeal GroEL/GroES system has preserved the basic encapsulation mechanism of bacterial GroEL and suggest that it has adjusted the length of its reaction cycle to the slower growth rates of Archaea. The release of only folded protein from the GroEL/GroES cage would avoid non-productive interactions of the GroEL substrates with the thermosome, which is not normally located within the same compartment ADP + phosphate + an unfolded polypeptide
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 ?

Organism

EC Number Organism UniProt Comment Textmining
5.6.1.7 Methanosarcina mazei
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.1.7 ATP + H2O + a folded polypeptide the archaeal GroEL/GroES system has preserved the basic encapsulation mechanism of bacterial GroEL and suggest that it has adjusted the length of its reaction cycle to the slower growth rates of Archaea. The release of only folded protein from the GroEL/GroES cage would avoid non-productive interactions of the GroEL substrates with the thermosome, which is not normally located within the same compartment Methanosarcina mazei ADP + phosphate + an unfolded polypeptide
-
 ?
5.6.1.7 ATP + H2O + a folded polypeptide optimal functionality of MmGroEL/GroES and its ability to encapsulate larger proteins, such as malate dehydrogenase, requires the presence of ammonium sulfate in vitro Methanosarcina mazei ADP + phosphate + an unfolded polypeptide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.6.1.7 GroEL/GroES chaperonin system
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 Methanosarcina mazei