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Literature summary for 5.6.1.7 extracted from

  • Melkani, G.C.; Zardeneta, G.; Mendoza, J.A.
    On the chaperonin activity of GroEL at heat-shock temperature (2005), Int. J. Biochem. Cell Biol., 37, 1375-1385.
    View publication on PubMed
Search for more literature for 5.6.1.7

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information GroEL interacts strongly with the enzyme rhodanese undergoing thermal unfolding at 43°C. The enzyme forms a binary complex. Active rhodanese (82%) could be recovered by releasing the enzyme from GroEL after the addition of several components, e.g. ATP and the co-chaperonin GroES. The inability to recover active enzyme at 43°C from the GroEL–rhodanese complex is not due to the disruption of the complex or aggregation of rhodanese, but rather to the partial loss of its ATPase activity and/or to the inability of rhodanese to be released from GroEL due to a conformational change Escherichia coli ?
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Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
43
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 GroEL interacts strongly with the enzyme rhodanese undergoing thermal unfolding at 43°C. The enzyme forms a binary complex. Active rhodanese (82%) could be recovered by releasing the enzyme from GroEL after the addition of several components, e.g. ATP and the co-chaperonin GroES. The inability to recover active enzyme at 43°C from the GroEL–rhodanese complex is not due to the disruption of the complex or aggregation of rhodanese, but rather to the partial loss of its ATPase activity and/or to the inability of rhodanese to be released from GroEL due to a conformational change Escherichia coli