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Literature summary for 3.4.21.92 extracted from

  • Wojtkowiak, D.; Geogopoulos, C.; Zylicz, M.
    Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli (1993), J. Biol. Chem., 268, 22609-22617.
    View publication on PubMed
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
 x * 46000, ClpX, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 W3110 B178
-
Escherichia coli W3110 B178
-
 W3110 B178
-

Purification (Commentary)

Purification (Comment) Organism
ClpX Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli

Storage Stability

Storage Stability Organism
-15°C, 20% glycerol, 70% loss of activity after 1 month, subunit ClpX Escherichia coli
-70°C, stable without substantial loss of activity, subunit ClpX Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Bacteriophage lambdaO-DNA replication protein + H2O degraded by ClpXP Escherichia coli Hydrolyzed bacteriophage lambdaO-DNA replication protein
-
 ?
Bacteriophage lambdaO-DNA replication protein + H2O degraded by ClpXP Escherichia coli W3110 B178 Hydrolyzed bacteriophage lambdaO-DNA replication protein
-
 ?

Subunits

Subunits Comment Organism
? x * 46000, ClpX, SDS-PAGE Escherichia coli
More enzyme consists of two components: ClpP and ClpA or ClpX Escherichia coli
More ClpX participates with ClpP in the rapid and specific degradation of the lambda O protein Escherichia coli