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Literature summary for 5.6.1.7 extracted from

  • Melkani, G.C.; Sielaff, R.; Zardeneta, G.; Mendoza, J.A.
    Interaction of oxidized chaperonin GroEL with an unfolded protein at low temperatures (2012), Biosci. Rep., 32, 299-303.
    View publication on PubMed
Search for more literature for 5.6.1.7

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of chaperonin GroEL in Escherichia coli cells bearing the multicopy plasmid pGroESL Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information the refolding of urea-denatured rhodanese is catalzed at low temperatures by oxidized GroEL, which contains increased exposed hydrophobic surfaces and retains its ability to hydrolyse ATP, oxidation of GroEL with H2O2. Oxidized GroEL efficiently binds the urea-unfolded rhodanese at 4°C, without requiring excess amount of chaperonin relative to normal GroEL (i.e. non-oxidized). The oxidized GroEL has the potential to efficiently trap recombinant or non-native proteins at 4°C and release them at higher temperatures under appropriate conditions Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57259
-
 x * 57259, sequence calculation, x * 60000, recombinant enzyme, SDS-PAGE Escherichia coli
60000
-
 x * 57259, sequence calculation, x * 60000, recombinant enzyme, SDS-PAGE 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
-
 ADP + phosphate + an unfolded polypeptide
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant chaperonin GroEL from Escherichia coli 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
-
 ?
additional information the refolding of urea-denatured rhodanese is catalyzed by the wild-type enzyme, and also at low temperatures by oxidized GroEL, which contains increased exposed hydrophobic surfaces and retains its ability to hydrolyse ATP. Oxidized GroEL efficiently binds the urea-unfolded rhodanese at 4°C, without requiring excess amount of chaperonin relative to normal GroEL (i.e. non-oxidized). The loss of the ATPase activity of oxidized GroEL at 4°C prevents the release of rhodanese from the GroEL-rhodanese complex Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
? x * 57259, sequence calculation, x * 60000, recombinant enzyme, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
chaperonin GroEL
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22 37 release/reactivation of rhodanese from/by GroEL Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4 37 and above, the release/reactivation of rhodanese from/by GroEL is minimal at 4°C, but is optimal between 22°C and 37°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 assay at Escherichia coli

General Information

General Information Comment Organism
physiological function the chaperonin GroEL binds to non-native substrate proteins via hydrophobic interactions, preventing their aggregation, which is minimized at low temperatures Escherichia coli