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Literature summary for 5.6.1.7 extracted from

  • Khor, H.K.; Fisher, M.T.; Schoeneich, C.
    Potential role of methionine sulfoxide in the inactivation of the chaperone GroEL by hypochlorous acid (HOCl) and peroxynitrite(ONOO-) (2004), J. Biol. Chem., 279, 19486-19493.
    View publication on PubMed

General Stability

General Stability Organism
GroEL is rather insensitive to oxidants produced endogenously during metabolism, such as nitric oxide or hydrogen peroxide, but is efficiently modified and inactivated by reactive species generated by phagocytes, such as peroxynitrite and hypochlorous acid (HOCl). HOCl inactivates through the oxidation of methionine to methionine sulfoxide. In addition to the oxidation of methionine, HOCl causes the conversion of cysteine to cysteic acid and this product may account for the remainder of inactivated GroEL not recoverable through MsrB/A. HOCl produces only negligible yields of 3-chlorotyrosine. The high sensitivity of GroEL toward HOCl and ONOO suggests that this protein may be a target for bacterial killing by phagocytes Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide
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Escherichia coli ADP + phosphate + an unfolded polypeptide
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?
additional information enzyme catalyzes refolding of denatured malate dehydrogenase into the active form Escherichia coli ?
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?

Synonyms

Synonyms Comment Organism
GroEl
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Escherichia coli