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Literature summary for 3.4.21.107 extracted from

  • Iwanczyk, J.; Leong, V.; Ortega, J.
    Factors defining the functional oligomeric state of Escherichia coli DegP protease (2011), PLoS ONE, 6, e18944.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.107

Protein Variants

Protein Variants Comment Organism
S210A proteolytically inactive mutant Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Escherichia coli
-
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-casein + H2O
-
 Escherichia coli ?
-
 ?
beta-casein + H2O
-
 Escherichia coli ?
-
 ?
malate dehydrogenase + H2O
-
 Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
oligomer x * about 50000, SDS-PAGE. In the absence of substrate, DegP oligomerizes as a hexameric cage but in its presence DegP reorganizes into active 12- and 24-mer cages. The size of the substrate molecule is the main factor conditioning the oligomeric state adopted by the enzyme, while ther factors such as temperature, do not influence the oligomeric state Escherichia coli

Synonyms

Synonyms Comment Organism
DegP
-
 Escherichia coli
HtrA
-
 Escherichia coli
protease do
-
 Escherichia coli