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Literature summary for 5.6.1.7 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
Search for more literature for 5.6.1.7

Activating Compound

Activating Compound Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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 ?
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

Synonyms Comment Organism
GroEL/GroES chaperonin system
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 Methanosarcina mazei