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Literature summary for 3.4.21.107 extracted from

  • Laskowska, E.; Kuczynska-Wisnik, D.; Skorko-Glonek, J.; Taylor, A.
    Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro (1996), Mol. Microbiol., 22, 555-571.
    View publication on PubMed
Search for more literature for 3.4.21.107

Inhibitors

Inhibitors Comment Organism Structure
DnaJ chaperone protein Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ stimulates at 10 mM Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli involved in the degradation of damaged proteins, participate in removal of aggregated proteins ?
-
 ?
Protein + H2O Escherichia coli
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type, htrA22 and htrA63 mutant Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-casein + H2O
-
 Escherichia coli ?
-
 ?
additional information involved in the degradation of damaged proteins, participate in removal of aggregated proteins Escherichia coli ?
-
 ?
Protein + H2O
-
 Escherichia coli ?
-
 ?
Protein + H2O denatured proteins aggregate to form a distinct S fraction, one third of the isolated S fraction is converted to trichloroacetic acid-soluble products Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
DegP
-
 Escherichia coli
Do
-
 Escherichia coli
HtrA
-
 Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
37 45 enzyme is more efficient at 45°C than at 37°C Escherichia coli