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Literature summary for 3.4.21.B50 extracted from

  • Kolmar, H.; Waller, P.R.; Sauer, R.T.
    The DegP and DegQ periplasmic endoproteases of Escherichia coli: specificity for cleavage sites and substrate conformation (1996), J. Bacteriol., 178, 5925-5929.
    View publication on PubMed
Search for more literature for 3.4.21.B50

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 6 * 50000, SDS-PAGE Escherichia coli
50000
-
 12 * 50000, SDS-PAGE Escherichia coli
300000
-
 hexamer, gel filtration Escherichia coli
600000
-
 dodecamer, gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli DegQ may degrade transiently denatured proteins, unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and/or newly secreted proteins prior to folding and disulfide bond formation ?
-
 ?

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.
Arc-st11 repressor + H2O cleavage sites: Val22-/-Arg23, Val25-/-Ala25 and Val41-/-Met42 Escherichia coli ?
-
 ?
lambda-repressor variant 105 + H2O cleavage sites: Val36-/-Ala37, Val71-/-Ser72, Ile84-/-Tyr85, Val91-/-Ser92 Escherichia coli ?
-
 ?
additional information DegQ may degrade transiently denatured proteins, unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and/or newly secreted proteins prior to folding and disulfide bond formation Escherichia coli ?
-
 ?
additional information model substrates are cleaved at discrete Val/Xaa or Ile/Xaa sites Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
dodecamer 12 * 50000, SDS-PAGE Escherichia coli
hexamer 6 * 50000, SDS-PAGE Escherichia coli