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Literature summary for 5.6.1.7 extracted from

  • Chapman, E.; Farr, G.W.; Furtak, K.; Horwich, A.L.
    A small molecule inhibitor selective for a variant ATP-binding site of the chaperonin GroEL (2009), Bioorg. Med. Chem. Lett., 19, 811-813.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.7

Protein Variants

Protein Variants Comment Organism
D398K block of ATP hydrolysis Escherichia coli
I493C mutation in binding pocket of GroEL Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
EC3016 inhibits ATPase activity of mutant I493C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + a folded polypeptide Escherichia coli bovine rhodanese ADP + phosphate + an unfolded polypeptide
-
 ?
ATP + H2O + a folded polypeptide Escherichia coli pig heart malate dehydrogenase ADP + phosphate + an unfolded polypeptide
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6F5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide
-
 Escherichia coli ADP + phosphate + an unfolded polypeptide
-
 ?
ATP + H2O + a folded polypeptide bovine rhodanese Escherichia coli ADP + phosphate + an unfolded polypeptide
-
 ?
ATP + H2O + a folded polypeptide pig heart malate dehydrogenase Escherichia coli ADP + phosphate + an unfolded polypeptide
-
 ?

Synonyms

Synonyms Comment Organism
chaperonin
-
 Escherichia coli
chaperonin GroEL
-
 Escherichia coli